



@article {3237,
	title = {Atomic force microscopy measurements reveal multiple bonds between Helicobacter pylori blood group antigen binding adhesin and Lewis b ligand},
	journal = {Journal of the Royal Society, Interface / the Royal Society},
	volume = {11},
	year = {2014},
	month = {2014},
	url = {<Go to ISI>://MEDLINE:25320070},
	author = {Parreira, P. and Shi, Q. and Magalhaes, A. and Reis, C.A. and Bugaytsova, J. and Boren, T. and Leckband, D. and Martins, M.C.L.}
}
@article {3273,
	title = {Characterization of hLF1-11 immobilization onto chitosan ultrathin films, and its effects on antimicrobial activity},
	journal = {Acta Biomaterialia},
	volume = {10},
	year = {2014},
	note = {Cited By (since 1996):1Export Date: 21 November 2014},
	month = {2014},
	pages = {3513 - 3521},
	abstract = {hLF1-11 (GRRRRSVQWCA) is an antimicrobial peptide (AMP) with high activity against methicillin-resistant Staphylococcus aureus (MRSA), the most prevalent species in implant-associated infection. In this work, the effect of the surface immobilization on hLF1-11 antimicrobial activity was studied. Immobilization was performed onto chitosan thin films as a model for an implant coating due to its reported osteogenic and antibacterial properties. Chitosan thin films were produced by spin-coating on gold surfaces. hLF1-11 was immobilized onto these films by its C-terminal cysteine in an orientation that exposes the antimicrobial activity-related arginine-rich portion of the peptide. Two levels of exposure (with and without a polyethylene glycol (PEG) spacer) were analyzed. Covalent immobilization was further compared with the AMP physical adsorption onto chitosan films. Surfaces were characterized using ellipsometry, contact angle measurements, atomic force microscopy, infrared and X-ray photoelectron spectroscopies and using a fluorimetric assay for hLF1-11 quantification. Surface antimicrobial activity was assessed through surface adhesion and viability assays using an MRSA (S. aureus ATCC 33591). The incorporation of hLF1-11 increased significantly bacterial adhesion to chitosan films. However, the presence of hLF1-11, namely when immobilized through a PEG spacer, decreased the viability of adherent bacteria with regard to the control surface. These results demonstrated that hLF1-11 after covalent immobilization by its cysteine can maintain activity, particularly if a spacer is applied. However, further studies, exploring the opposite orientation or the same C-terminal orientation, but non-cysteine related, can help to clarify the potential of the hLF1-11 immobilization strategy. {\textcopyright} 2014 Acta Materialia Inc. Published by Elsevier Ltd. All rights reserved.},
	keywords = {Antimicrobial peptides (AMP), Bacterial adhesion, chitosan, Surface characterization, Surface immobilization},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84903724424\&partnerID=40\&md5=e8009cd480b49c37a991753cd145cf34},
	author = {Costa, F. and Maia, S. and Gomes, J. and Gomes, P. and Martins, M.C.L.}
}
@article {3294,
	title = {Eradication of Helicobacter pylori: Past, present and future},
	journal = {Journal of Controlled Release},
	volume = {189},
	year = {2014},
	note = {Export Date: 21 November 2014},
	month = {2014},
	pages = {169 - 186},
	abstract = {Helicobacter pylori is the major cause of chronic gastritis and peptic ulcers. Since the classification as a group 1 carcinogenic by International Agency for Research on Cancer, the importance of the complete H. pylori eradication has obtained a novel meaning. Hence, several studies have been made in order to deepen the knowledge in therapy strategies. However, the current therapy presents unsatisfactory eradication rates due to the lack of therapeutic compliance, antibiotic resistance, the degradation of antibiotics at gastric pH and their insufficient residence time in the stomach. Novel approaches have been made in order to overcome these limitations. The purpose of this review is to provide an overview about the current therapy and its limitations, while highlighting the possibility of using micro- and nanotechnology to develop gastric drug delivery systems, overcoming these difficulties in the future. {\textcopyright} 2014 Elsevier B.V.},
	keywords = {Drug delivery, Helicobacter pylori, Microparticles, nanoparticles, Treatment},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84904904149\&partnerID=40\&md5=96cfe2d7f96a7c7a16bb7eb733c2b71c},
	author = {Lopes, D. and Nunes, C. and Martins, M.C.L. and Sarmento, B. and Reis, S.}
}
@article {3289,
	title = {The potential utility of chitosan micro/nanoparticles in the treatment of gastric infection},
	journal = {Expert Review of Anti-Infective Therapy},
	volume = {12},
	year = {2014},
	note = {Export Date: 21 November 2014},
	month = {2014},
	pages = {981 - 992},
	abstract = {Gastric infections are mainly caused by Helicobacter pylori (H. pylori), a bacterium that colonizes the gastric mucosa of over 50\% of the world{\textquoteright}s population. Chronic H. pylori infection has been associated with gastric diseases such as chronic gastritis, peptic ulcer and gastric adenocarcinoma. Current eradication treatment relies on antibiotic-based therapies that are unsuccessful in approximately 20\% of the patients. Chitosan, a natural and cationic polysaccharide has been investigated in the treatment of H. pylori infection. Due to its mucoadhesive properties, it has been used in the form of micro/nanoparticles, polyelectrolyte complexes or coatings as antibiotic encapsulation systems for gastric delivery, but alternative molecules may also be incorporated. It has been recently proposed that chitosan can also be used for H. pylori binding and scavenging from the host stomach due to its antimicrobial/binding properties. In this manuscript, a brief description of the use of chitosan in H. pylori treatment is reviewed. {\textcopyright} Informa UK, Ltd.},
	keywords = {Biomaterials, chitosan, Crosslinking, Drug delivery, Gastric cancer, Helicobacter pylori, Microspheres, mucoadhesion, nanoparticles, Polyelectrolytes},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84904003586\&partnerID=40\&md5=d8a682d7ce6be8633b1505d0a7b8adae},
	author = {Gon{\c c}alves, I.C. and Henriques, P.C. and Seabra, C.L. and Martins, M.C.L.}
}
@article {3285,
	title = {Selective albumin-binding surfaces modified with a thrombin-inhibiting peptide},
	journal = {Acta Biomaterialia},
	volume = {10},
	year = {2014},
	note = {Export Date: 21 November 2014},
	month = {2014},
	pages = {1227 - 1237},
	abstract = {Blood-contacting medical devices have been associated with severe clinical complications, such as thrombus formation, triggered by the activation of the coagulation cascade due to the adsorption of certain plasma proteins on the surface of biomaterials. Hence, the coating of such surfaces with antithrombotic agents has been used to increase biomaterial haemocompatibility. Biomaterial-induced clotting may also be decreased by albumin adsorption from blood plasma in a selective and reversible way, since this protein is not involved in the coagulation cascade. In this context, this paper reports that the immobilization of the thrombin inhibitor D-Phe-Pro-D-Arg-D-Thr-CONH 2 (fPrt) onto nanostructured surfaces induces selective and reversible adsorption of albumin, delaying the clotting time when compared to peptide-free surfaces. fPrt, synthesized with two glycine residues attached to the N-terminus (GGfPrt), was covalently immobilized onto self-assembled monolayers (SAMs) having different ratios of carboxylate-hexa(ethylene glycol)- and tri(ethylene glycol)-terminated thiols (EG6-COOH/EG3) that were specifically designed to control GGfPrt orientation, exposure and density at the molecular level. In solution, GGfPrt was able to inactivate the enzymatic activity of thrombin and to delay plasma clotting time in a concentration-dependent way. After surface immobilization, and independently of its concentration, GGfPrt lost its selectivity to thrombin and its capacity to inhibit thrombin enzymatic activity against the chromogenic substrate n-p-tosyl-Gly-Pro-Arg-p-nitroanilide. Nevertheless, surfaces with low concentrations of GGfPrt could delay the capacity of adsorbed thrombin to cleave fibrinogen. In contrast, GGfPrt immobilized in high concentrations was found to induce the procoagulant activity of the adsorbed thrombin. However, all surfaces containing GGfPrt have a plasma clotting time similar to the negative control (empty polystyrene wells), showing resistance to coagulation, which is explained by its capacity to adsorb albumin in a selective and reversible way. This work opens new perspectives to the improvement of the haemocompatibility of blood-contacting medical devices. {\textcopyright} 2013 Acta Materialia Inc. Published by Elsevier Ltd. All rights reserved.},
	keywords = {Albumin, Blood compatibility, Clotting, Surface modification, Thrombin},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84895067841\&partnerID=40\&md5=8486186625f8f4f1cbc538bb3e34dd82},
	author = {Freitas, S.C. and Maia, S. and Figueiredo, A.C. and Gomes, P. and Pereira, P.J.B. and Barbosa, M.A. and Martins, M.C.L.}
}
@article {2759,
	title = {Adsorbed fibrinogen leads to improved bone regeneration and correlates with differences in the systemic immune response},
	journal = {Acta Biomaterialia},
	volume = {9},
	year = {2013},
	note = {Export Date: 23 May 2013Source: ScopusArticle in Press},
	month = {07/2013},
	pages = {7209-7217},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84876834487\&partnerID=40\&md5=2d00f0bc55f461c9c979548276f0e53d},
	author = {Santos, S.G. and Lamghari, M. and Almeida, C.R. and Oliveira, M.I. and Neves, N. and Ribeiro, A.C. and Barbosa, J.N. and Barros, R. and Maciel, J. and Martins, M.C.L. and Gon{\c c}alves, R.M. and Barbosa, M.A.}
}
@booklet {2829,
	title = {Bacterial-binding chitosan microspheres for gastric infection treatment and prevention},
	howpublished = {Acta Biomaterialia},
	volume = {9},
	year = {2013},
	note = {Export Date: 12 December 2013Source: Scopus},
	month = {2013///},
	pages = {9370 - 9378},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84887160912\&partnerID=40\&md5=dd414f3b1e57bee7c37bc37a44983d27},
	author = {Gon{\c c}alves, I.C. and Magalh{\~a}es, A. and Fernandes, M. and Rodrigues, I.V. and Reis, C.A. and Martins, M.C.L.}
}
@article {2835,
	title = {Bioengineered surfaces promote specific protein-glycan mediated binding of the gastric pathogen Helicobacter pylori},
	journal = {Acta Biomaterialia},
	volume = {9},
	year = {2013},
	note = {Export Date: 12 December 2013Source: Scopus},
	month = {2013///},
	pages = {8885 - 8893},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84885052038\&partnerID=40\&md5=0d17eb0f95d76eb18ea20ef7f33c8192},
	author = {Parreira, P. and Magalh{\~a}es, A. and Reis, C.A. and Bor{\'e}n, T. and Leckband, D. and Martins, M.C.L.}
}
@article {2885,
	title = {Effect of gastric environment on Helicobacter pylori adhesion to a mucoadhesive polymer},
	journal = {Acta Biomaterialia},
	volume = {9},
	year = {2013},
	note = {Cited By (since 1996):2Export Date: 12 December 2013Source: Scopus},
	month = {2013///},
	pages = {5208 - 5215},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84872069015\&partnerID=40\&md5=22eea6321dd7764e20a4460b47a72ba8},
	author = {Nogueira, F. and Gon{\c c}alves, I.C. and Martins, M.C.L.}
}
@article {2847,
	title = {Modulation of stability and mucoadhesive properties of chitosan microspheres for therapeutic gastric application},
	journal = {International Journal of Pharmaceutics},
	volume = {454},
	year = {2013},
	note = {Cited By (since 1996):1Export Date: 12 December 2013Source: Scopus},
	month = {2013///},
	pages = {116 - 124},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84884163785\&partnerID=40\&md5=1d040067777b023c63bb769260b66dcd},
	author = {Fernandes, M. and Gon{\c c}alves, I.C. and Nardecchia, S. and Amaral, I.F. and Barbosa, M.A. and Martins, M.C.L.}
}
@booklet {2190,
	title = {Bioengineered surfaces to improve the blood compatibility of biomaterials through direct thrombin inactivation},
	howpublished = {Acta BiomaterialiaActa Biomater.},
	year = {2012},
	note = {Export Date: 21 November 2012Source: ScopusArticle in Pressdoi: 10.1016/j.actbio.2012.07.020Language of Original Document: EnglishCorrespondence Address: Martins, M.C.L.; INEB - Instituto de Engenharia Biom{\'e}dica, Universidade do Porto, Rua do Campo Alegre 823, 415email: cmartins@ineb.up.pt},
	month = {2012///},
	abstract = {Thrombus formation, due to thrombin generation, is a major problem affecting blood-contacting medical devices. This work aimed to develop a new strategy to improve the hemocompatibility of such devices by the immobilization of a naturally occurring thrombin inhibitor into a nanostructured surface. Boophilin, a direct thrombin inhibitor from the cattle tick Rhipicephalus microplus, was produced as a recombinant protein in Pichia pastoris. Boophilin was biotinylated and immobilized on biotin-terminated self-assembled monolayers (SAM) via neutravidin. In order to maintain its proteinase inhibitory capacity after surface immobilization, boophilin was biotinylated after the formation of a boophilin-thrombin complex to minimize the biotinylation of the residues involved in thrombin-boophilin interaction. The extent of boophilin biotinylation was determined using matrix-assisted laser desorption/ionization-time of flight/time of flight mass spectrometry. Boophilin immobilization and thrombin adsorption were quantified using quartz crystal microbalance with dissipation. Thrombin competitive adsorption from human serum was assessed using                        125I-thrombin. Thrombin inhibition and plasma clotting time were determined using spectrophotometric techniques. Boophilin-coated SAM were able to promote thrombin adsorption in a selective way, inhibiting most of its activity and delaying plasma coagulation in comparison with boophilin-free surfaces, demonstrating boophilin{\textquoteright}s potential to improve the hemocompatibility of biomaterials used in the production of blood-contacting devices. {\textcopyright} 2012 Acta Materialia Inc.
},
	keywords = {Coagulation, Hemocompatibility, Protein adsorption, Surface functionalization, Thrombin},
	isbn = {17427061 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84865246462\&partnerID=40\&md5=278b2e7d1427a6032eba9ecbd01c3872},
	author = {Freitas, S.C. and Cereija, T.B. and Figueiredo, A.C. and Os{\'o}rio, H. and Pereira, P.J.B. and Barbosa, M.A. and Martins, M.C.L.}
}
@booklet {2186,
	title = {Effect of gastric environment on Helicobacter pylori adhesion to a mucoadhesive polymer},
	howpublished = {Acta BiomaterialiaActa Biomater.},
	year = {2012},
	note = {Export Date: 21 November 2012Source: ScopusArticle in Pressdoi: 10.1016/j.actbio.2012.09.011Language of Original Document: EnglishCorrespondence Address: Martins, M.C.L.; INEB-Instituto de Engenharia Biom{\'e}dica, Universidade do Porto, Rua do Campo Alegre, 823, 4150email: cmartins@ineb.up.pt},
	month = {2012///},
	abstract = {Helicobacter pylori infection has been associated with several gastric diseases. This bacterium colonizes the gastric mucosa of half of the world{\textquoteright}s population, and available treatments are unsuccessful in practically one in every five patients. Mucoadhesive polymers, such as chitosan, are being investigated as gastric drug delivery systems. However, since chitosan is also known for its antimicrobial properties, this work aims to evaluate H. pylori interactions with chitosan under simulated gastric environments, namely using various pHs (2.6, 4 and 6), pepsin and urea. To enable the visualization of adherent bacteria, ultrathin chitosan films were produced by spin-coating on gold/glass surfaces, cross-linked with genipin and characterized by Fourier transform infrared reflection absorption spectroscopy, ellipsometry and electrokinetic analysis. Films with homogeneous thickness of 11.7 {\textpm} 0.6 nm were produced, and were stable and protonated at all the pHs used. Furthermore, they adsorbed pepsin in all these pHs, in contrast to urea, of which a small adsorption was only observed at pH 6. H. pylori binding to chitosan was higher at pH 2.6 although most of adherent bacteria were dead. The presence of pepsin decreased bacterial adhesion, but increased its viability while in a more stressed morphology (coccoid form). The presence of urea did not affect the amount, morphology or viability of chitosan-adherent bacteria. In suspension, the decrease in pH changed H. pylori zeta potential from negative to positive. Moreover, bacteria were only culturable when incubated in pH 6 with and without urea (without pepsin). This work demonstrates that chitosan has the capacity to bind and kill H. pylori in a range of pHs independently of urea. This opens new perspectives for the application of chitosan-based materials to the elimination of H. pylori gastric colonization, though pepsin might appear to be an obstacle. {\textcopyright} 2012 Acta Materialia Inc.},
	keywords = {Bacterial adhesion, Biomaterials, chitosan, Helicobacter pylori, Thin films},
	isbn = {17427061 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84867507239\&partnerID=40\&md5=defd903a9833b81e1d4e9e377550ce07},
	author = {Nogueira, F. and Gon{\c c}alves, I.C. and Martins, M.C.L.}
}
@article {2212,
	title = {Synthesis of an O-alkynyl-chitosan and its chemoselective conjugation with a PEG-like amino-azide through click chemistry},
	journal = {Carbohydrate PolymersCarbohydr Polym},
	volume = {87},
	year = {2012},
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},
	month = {2012///},
	pages = {240 - 249},
	abstract = {N-Phthaloyl-chitosan O-prop-2-ynyl carbamate was prepared as a biopolymer amenable to undergo chemoselective conjugation by azide-alkyne coupling, while allowing upturn of chitosan{\textquoteright}s amines after dephthaloylation. N-phthaloylchitosan was prepared according to previously described methods and, due to its low solubility in current organic media, subsequent modifications were run in heterogeneous conditions. Activation of hydroxyls with carbonyl-1,1'- diimidazole and coupling to propargylamine yielded N-phthaloyl-chitosan O-prop-2-ynyl carbamate, then coupled to a model PEG-like azide by azide-alkyne coupling, giving the expected triazolyl conjugate. N-Dephthaloylation allowed recovery of the free amines, responsible for chitosan{\textquoteright}s bioadhesion and tissue-regeneration properties. The structures of all polymers were confirmed by Fourier-transformed infra-red (FT-IR) and X-ray photoelectron (XPS) spectroscopies, as well as by solid-state nuclear magnetic resonance (SSNMR). All chitosan derivatives were poorly soluble in both aqueous and organic media, which makes them suitable for topical applications or for removal of toxic substances from either the gastric intestinal tract or environmental sources. {\textcopyright} 2011 Elsevier Ltd. All Rights Reserved.},
	keywords = {1 ,3-Dipolarcycloaddition, Acetylene, Amines, Azide-alkyne coupling, Bio-adhesion, Bioadhesion, Biomaterials, chitosan, click chemistry, Cycloaddition, FTIR, Huisgen{\textquoteright}s 1,3-dipolar cycloaddition, Nuclear magnetic resonance, Nuclear magnetic resonance spectroscopy, Photoelectron spectroscopy, Resonance, Size exclusion chromatography, Size-exclusion chromatography, Solid state NMR, Solid-state NMR, Tissue, X ray photoelectron spectroscopy, XPS},
	isbn = {01448617 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-80054771159\&partnerID=40\&md5=3760f41563573759f0ce676fe813d6c6},
	author = {Oliveira, J.R. and Martins, M.C.L. and Mafra, L. and Gomes, P.}
}
@article {2236,
	title = {Covalent immobilization of antimicrobial peptides (AMPs) onto biomaterial surfaces},
	journal = {Acta BiomaterialiaActa Biomater.},
	volume = {7},
	year = {2011},
	note = {Cited By (since 1996): 24Export Date: 21 November 2012Source: Scopusdoi: 10.1016/j.actbio.2010.11.005PubMed ID: 21056701Language of Original Document: EnglishCorrespondence Address: Martins, M. C. L.; INEB - Instituto de Engenharia Biom{\'e}dica, Divis{\~a}o de Biomateriais, Universidade Do Porto, Rua do Campo Alegre 823, 4150-180 Porto, Portugal; email: cmartins@ineb.up.ptChemicals/CAS: amoxicillin, 26787-78-0, 34642-77-8, 61336-70-7; ampicillin, 69-52-3, 69-53-4, 7177-48-2, 74083-13-9, 94586-58-0; carbenicillin, 17230-86-3, 4697-36-3, 4800-94-6; cefazolin, 25953-19-9, 27164-46-1; gentamicin, 1392-48-9, 1403-66-3, 1405-41-0; penicillin G, 1406-05-9, 61-33-6; teicoplanin, 61036-62-2, 61036-64-4; tobramycin, 32986-56-4; vancomycin, 1404-90-6, 1404-93-9; Antimicrobial Cationic Peptides; Biocompatible Materials; Coated Materials, Biocompatible; Immobilized ProteinsReferences: Glinel, K., Jonas, A.M., Jouenne, T., Leprince, J., Galas, L., Huck, W.T., Antibacterial and antifouling polymer brushes incorporating antimicrobial peptide (2009) Bioconj Chem, 20 (1), pp. 71-77;Vila, J., Soriano, A., Mensa, J., Molecular basis of microbial adherence to prosthetic materials. Role of biofilms in prosthesis-associated infection (2008) Enferm Infecc Microbiol Clin, 26 (1), pp. 48-54; 
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},
	month = {2011///},
	pages = {1431 - 1440},
	abstract = {Bacterial adhesion to biomaterials remains a major problem in the medical devices field. Antimicrobial peptides (AMPs) are well-known components of the innate immune system that can be applied to overcome biofilm-associated infections. Their relevance has been increasing as a practical alternative to conventional antibiotics, which are declining in effectiveness. The recent interest focused on these peptides can be explained by a group of special features, including a wide spectrum of activity, high efficacy at very low concentrations, target specificity, anti-endotoxin activity, synergistic action with classical antibiotics, and low propensity for developing resistance. Therefore, the development of an antimicrobial coating with such properties would be worthwhile. The immobilization of AMPs onto a biomaterial surface has further advantages as it also helps to circumvent AMPs{\textquoteright} potential limitations, such as short half-life and cytotoxicity associated with higher concentrations of soluble peptides. The studies discussed in the current review report on the impact of covalent immobilization of AMPs onto surfaces through different chemical coupling strategies, length of spacers, and peptide orientation and concentration. The overall results suggest that immobilized AMPs may be effective in the prevention of biofilm formation by reduction of microorganism survival post-contact with the coated biomaterial. Minimal cytotoxicity and long-term stability profiles were obtained by optimizing immobilization parameters, indicating a promising potential for the use of immobilized AMPs in clinical applications. On the other hand, the effects of tethering on mechanisms of action of AMPs have not yet been fully elucidated. Therefore, further studies are recommended to explore the real potential of immobilized AMPs in health applications as antimicrobial coatings of medical devices. {\textcopyright} 2010 Acta Materialia Inc. Published by Elsevier Ltd. All rights reserved.},
	keywords = {Amino Acid Sequence, amoxicillin, ampicillin, Animals, antibiotic agent, antibiotic resistance, Antimicrobial Cationic Peptides, Antimicrobial peptides, Bacteria (microorganisms), Bacterial adhesion, bacterial survival, Biocompatible Materials, biofilm, Biofilms, biomaterial, carbenicillin, cefazolin, Coated Materials, Biocompatible, Cytotoxicity, drug activity, drug half life, drug solubility, drug stability, drug targeting, gentamicin, human, Humans, Immobilized Proteins, Molecular Sequence Data, mouth inflammation, Nanostructured surfaces, nonhuman, penicillin G, polypeptide antibiotic agent, priority journal, review, sepsis, skin infection, soft tissue infection, Surface functionalization, Surface Properties, teicoplanin, tobramycin, vancomycin},
	isbn = {17427061 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-79952187401\&partnerID=40\&md5=70d486a4c6e1ba88f804c0f0d4f4e510},
	author = {Costa, F. and Carvalho, I.F. and Montelaro, R.C. and Gomes, P. and Martins, M.C.L.}
}
@article {2232,
	title = {Interactions of leukocytes and platelets with poly(lysine/leucine) immobilized on tetraethylene glycol-terminated self-assembled monolayers},
	journal = {Acta BiomaterialiaActa Biomater.},
	volume = {7},
	year = {2011},
	note = {Cited By (since 1996): 3Export Date: 21 November 2012Source: Scopusdoi: 10.1016/j.actbio.2011.01.013PubMed ID: 21237292Language of Original Document: EnglishCorrespondence Address: Martins, M. C. L.; Instituto de Engenharia Biom{\'e}dica, Divis{\~a}o de Biomateriais, Universidade Do Porto, Rua do Campo Alegre, 823, 4150-180 Porto, Portugal; email: cmartins@ineb.up.ptChemicals/CAS: heparin, 37187-54-5, 8057-48-5, 8065-01-8, 9005-48-5; leucine, 61-90-5, 7005-03-0; polylysine, 25104-18-1, 25988-63-0, 33960-24-6, 38000-06-5, 73565-56-7; Ethylene Glycol, 107-21-1; Imidazoles; Immobilized Proteins; N,N-carbonyldiimidazole, 530-62-1; Polyethylene Glycols; Polylysine, 25104-18-1; ProteinsReferences: Dailey, J., (1998) Blood, , 2nd ed. Ipswich (MA, USA): Medical Consulting Group;Section V: Chronic intermittent haemodialysis and prevention of clotting in the extracorporal system (2002) Nephrol Dial Transplant, 17 (SUPPL. 7), pp. 63-71. , European Best Practice Guidelines Working Group; 
Martins, M.C., Curtin, S.A., Freitas, S.C., Salgueiro, P., Ratner, B.D., Barbosa, M.A., Molecularly designed surfaces for blood deheparinization using an immobilized heparin-binding peptide (2009) J Biomed Mater Res A, 88, pp. 162-173; 
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Rodrigues, S.N., Goncalves, I.C., Martins, M.C.L., Barbosa, M.A., Ratner, B.D., Fibrinogen adsorption, platelet adhesion and activation on mixed hydroxyl-/methyl-terminated self-assembled monolayers (2006) Biomaterials, 27 (31), pp. 5357-5367. , DOI 10.1016/j.biomaterials.2006.06.010, PII S0142961206005515; 
Goncalves, I.C., Martins, M.C., Barbosa, M.A., Naeemi, E., Ratner, B.D., Selective protein adsorption modulates platelet adhesion and activation to oligo(ethylene glycol)-terminated self-assembled monolayers with C18 ligands (2009) J Biomed Mater Res, 89 A, pp. 642-653; 
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Barbosa, J.N., Martins, M.C.L., Freitas, S.C., Goncalves, I.C., Aguas, A.P., Barbosa, M.A., Adhesion of human leucocytes on mixtures of hydroxyl- and methyl-terminated self-assembled monolayers: Effect of blood protein adsorption (2010) J Biomed Mater Res, 93 A, pp. 12-19; 
Sperling, C., Schweiss, R.B., Streller, U., Werner, C., In vitro hemocompatibility of self-assembled monolayers displaying various functional groups (2005) Biomaterials, 26, pp. 6547-6557; 
Toda, M., Kitazawa, T., Hirata, I., Hirano, Y., Iwata, H., Complement activation on surfaces carrying amino groups (2008) Biomaterials, 29 (4), pp. 407-417. , DOI 10.1016/j.biomaterials.2007.10.005, PII S014296120700796X
},
	month = {2011///},
	pages = {1949 - 1955},
	abstract = {Surfaces that bind heparin are important for biomaterials for blood deheparinization. In our recent work it was demonstrated that a polypeptide composed of l-lysine and l-leucine (pKL), after immobilization onto tetra(ethylene glycol) terminated self-assembled monolayers (EG4-SAMs), can bind heparin from blood plasma in a selective, concentration-dependent way. During this work the effect of this peptide on platelet adhesion and activation and leukocyte adhesion was studied. The surface charge of these nanostructured surfaces was evaluated in order to correlate the effect of positively charged amine groups and hydrophobic methyl groups on the behavior of platelets and leukocyte adhesion. The results demonstrated that the presence of pKL decreased leukocyte adhesion to EG4-SAMs at all concentrations used. This effect is even more pronounced when surfaces were pre-immersed in heparinized plasma. In contrast, there is an increase in platelet adhesion and activation with increased percentage immobilized pKL. This effect is enhanced when surfaces were pre-immersed in heparinized plasma. However, adsorbed pKL in very low amounts does not induce platelet adhesion and activation compared with EG4, even when pre-immersed in plasma. Since only low pKL amounts are necessary to induce heparin selectivity, these results are promising for the development of heparin-binding biomaterials for blood deheparinization. {\textcopyright} 2011 Acta Materialia Inc. Published by Elsevier Ltd. All rights reserved.},
	keywords = {article, Blood Platelets, Cell Communication, Cell Shape, Ethylene Glycol, heparin, heparin binding protein, Humans, hydrophobicity, Imidazoles, Immobilized Proteins, leucine, leukocyte, leukocyte adherence, Leukocytes, methyl group, nanomaterial, plasma, Platelet Adhesiveness, Platelets, Polyethylene Glycols, polylysine, polypeptide, priority journal, Proteins, self assembled monolayer, Self-assembled monolayers, static electricity, Surface charge, Surface Properties, Tetra, thrombocyte, thrombocyte adhesion},
	isbn = {17427061 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-79953868334\&partnerID=40\&md5=2cb5b44223fe6e8106b513b80689103d},
	author = {Martins, M.C.L. and Ochoa-Mendes, V. and Ferreira, G. and Barbosa, J.N. and Curtin, S.A. and Ratner, B.D. and Barbosa, M.A.}
}
@article {2281,
	title = {Adhesion of human leukocytes on mixtures of hydroxyl- and methyl-terminated self-assembled monolayers: Effect of blood protein adsorption},
	journal = {Journal of Biomedical Materials Research - Part AJ. Biomed. Mater. Res. Part A},
	volume = {93},
	year = {2010},
	note = {Cited By (since 1996): 4Export Date: 21 November 2012Source: ScopusCODEN: JBMRCdoi: 10.1002/jbm.a.32480PubMed ID: 19484768Language of Original Document: EnglishCorrespondence Address: Barbosa, J. N.; Divis{\~a}o de Biomateriais, INEB-Instituto de Engenharia Biom{\'e}dica, Universidade do Porto, Porto 4150-180, Portugal; email: judite@ineb.up.ptChemicals/CAS: Blood Proteins; Gold, 7440-57-5; Hydroxyl Radical, 3352-57-6References: Brodbeck, W.G., Nakayama, Y., Matsuda, T., Colton, E., Ziats, N.P., Anderson, J.M., Biomaterial surface chemistry dictates adherent monocyte/macrophage cytokine expression in vitro (2002) Cytokine, 18, pp. 311-319;Kao, W.Y.J., Evaluation of leukocyte adhesion on polyurethanes: The effects of shear stress and blood proteins (2000) Biomaterials, 21, pp. 2295-2303; 
Tegoulia, V.A., Cooper, S.L., Leukocyte adhesion on model surfaces under flow: Effects of surface chemistry, protein adsorption, and shear rate (2000) J Biomed Mater Res, 50, pp. 291-301; 
Nimeri, G., Ohman, L., Elwing, H., Wettero, J., Bengtsson, T., The influence of plasma proteins and platelets on oxygen radical production and F-actin distribution in neutrophils adhering to polymer surfaces (2002) Biomaterials, 23, pp. 1785-1795; 
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Martins, M.C.L., Ratner, B.D., Barbosa, M.A., Protein adsorption on mixtures of hydroxyl- and methylterminated alkanethiols self-assembled monolavers (2003) J Biomed Mater Res, 67 A, pp. 158-171. , Part A; 
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Wettero, J., Bengtsson, T., Tengvall, P., Complement activation on immunoglobulin G-coated hydrophobic surfaces enhances the release of oxygen radicals from neutrophils through an actin-dependent mechanism (2000) J Biomed Mater Res, 51, pp. 742-751; 
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Barbosa, J.N., Barbosa, M.A., Aguas, A.P., Inflammatory responses and cell adhesion to self-assembled monolayers of alkanethiolates on gold (2004) Biomaterials, 25, pp. 2557-2563; 
Barbosa, J.N., Barbosa, M.A., Aguas, A.P., Inflammatory cell recruitment and adhesion to methyl-terminated selfassembled monolayers: Effect of implantation time (2005) Microsc Res Tech, 66, pp. 37-42; 
Barbosa, J.N., Madureira, P., Barbosa, M.A., Aguas, A.P., The attraction of Mac-1(+) phagocytes during acute inflammation by methyl-coated self-assembled monolayers (2005) Biomaterials, 26, pp. 3021-3027
},
	month = {2010///},
	pages = {12 - 19},
	abstract = {The adhesion of human leukocytes to nanostructured surfaces with different chemical properties and the effect of protein adsorption were investigated. Selfassembled monolayers (SAMs) prepared with mixtures of methyl- and hydroxyl-terminated alkanethiols in different percentages on gold were used. The surfaces were preimmersed in distinct protein solutions (human serum albumin, human fibrinogen, and autologous plasma). Adherent leukocytes were analyzed both by light and SEM. SAMs submitted to pre-immersion in plasma presented higher numbers of adherent leukocytes in the pure OH-terminated SAM, whereas methyl-terminated surfaces accounted for the lowest number of adherent cells. We observed a general increase in the number of adherent human leukocytes as the percentage of OH groups on the surface of the SAMs increased for all the pre-immersion conditions investigated. The number of adherent human leukocytes is highly influenced by the pre-immersion conditions used, and this observation is particularly relevant in the case of the methyl-terminated SAMs. The results obtained demonstrate that surface chemistry has a major influence in leukocyte adhesion to biomaterials, and that pre-immersion in protein solutions has a determinant effect in leukocyte adhesion. {\textcopyright} 2009 Wiley Periodicals, Inc.},
	keywords = {Adherent cells, Adhesion, Adsorption, Alkanethiols, article, Biological materials, biomaterial, Blood protein adsorption, Blood Proteins, cell adhesion, Cell Count, Chemical properties, gold, human, human cell, Human leukocytes, Human serum albumins, Humans, hydroxyl group, Hydroxyl Radical, Hydroxyl-terminated, immersion, Inflammatory response, leukocyte adherence, Leukocyte adhesion, Leukocytes, Nanostructured materials, Nanostructured surface, Nanostructured surfaces, OH group, Protein adsorption, protein blood level, Protein solution, Proteins, Sams, Scanning electron microscopy, Self assembled monolayers, Self-assembled monolayers, SEM, Surface chemistry, Surface Properties},
	isbn = {15493296 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-77649225392\&partnerID=40\&md5=0b35403e1b98581c557435b6cf7a8286},
	author = {Barbosa, J.N. and Martins, M.C.L. and Freitas, S.C. and Gon{\c c}alves, I.C. and {\'A}guas, A.P. and Barbosa, M.A.}
}
@article {2268,
	title = {Bioactivity of immobilized EGF on self-assembled monolayers: Optimization of the immobilization process},
	journal = {Journal of Biomedical Materials Research - Part AJ. Biomed. Mater. Res. Part A},
	volume = {94},
	year = {2010},
	note = {Cited By (since 1996): 7Export Date: 21 November 2012Source: ScopusCODEN: JBMRCdoi: 10.1002/jbm.a.32723PubMed ID: 20198690Language of Original Document: EnglishCorrespondence Address: Gon{\c c}alves, R.; INEB, Biomaterials Division, NEWTherapies Group, R. Campo Alegre, 823, Porto 4150-180, Portugal; email: raquelg@ineb.up.ptChemicals/CAS: epidermal growth factor, 62229-50-9; gold, 7440-57-5; Biocompatible Materials; Epidermal Growth Factor, 62229-50-9; Gold, 7440-57-5; Imidazoles; N,N-carbonyldiimidazole, 530-62-1; Polyethylene Glycols; Receptor, Epidermal Growth Factor, 2.7.10.1; Sulfhydryl CompoundsReferences: Singh, A., Harris, R.C., Autocrine, paracrine and juxtacrine signaling by EGFR ligands (2005) Cell Signal, 17, pp. 1183-1193;Luca, A., Carotenuto, A., Rachiglio, A., Gallo, M., Maiello, M.R., Aldinucci, D.L., Pinto, A., Normanno, N., The role of the EGFR signaling in tumor microenvironment (2008) J Cell Physiol, 214, pp. 559-567; 
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},
	month = {2010///},
	pages = {576 - 585},
	abstract = {Last trends in Biomaterials focus the mimic of cellular environments capable to control cellular responses. Epidermal growth factor (EGF) is a pleiotropic cytokine known to regulate cell proliferation, differentiation, and death. This study aims to optimize the immobilization of EGF on 11-mercapto-1-undecyl-tetra(ethylene)glycol (EG4) - self-assembled monolayers (SAMs) and to establish a new model surface to study EGF-mediated signaling. Gold substrates were modified with a monolayer of EG4 and N,N'- carbonyldiimidazole (CDI) was used to activate hydroxyl terminated groups of EG4-SAMs. EGF was then immobilized on activated EG4-SAMs at pH 7.4, 4{\textdegree}C, and 100 rpm. Different immobilization reaction times were tested as well as different CDI concentrations to optimize the reaction conditions and obtain a range of immobilized EGF concentrations on the surfaces. Surface characterization of EGF-SAMs was performed using radiolabeling, water contact angle measurements, X-ray photoelectron spectroscopy, and ELISA. Phosphorylation of EGFR on BT-20 breast cancer cell line by EGF-SAMs was tested by immunostaining. EGF was successfully immobilized on EG4-SAMs, at 4{\textdegree}C and pH 7.4 in a range of concentrations from 3.6 {\textpm} 0.8 to 17.6 {\textpm} 1.5 ng/cm                        2. The concentration of EGF increases with immobilization time and with the CDI concentration reaching the maximum for surfaces activated with 30 mg/mL of CDI after 48 h. The bioactivity of EGF-SAMs was confirmed by immunostaining of phospho-EGFR of BT-20 cells. This study described EGF immobilization on EG4-SAMs at different concentrations, which could be important surface models to study specific protein interactions at the molecular level evolving EGF-family of proteins. {\textcopyright} 2010 Wiley Periodicals, Inc. J.
},
	keywords = {Adsorption, Angle measurement, article, Biocompatible Materials, Biological materials, Breast cancer cells, cancer cell culture, Carbonyldiimidazole, Cell culture, Cell immobilization, Cell Line, Tumor, cell proliferation, Cellular environment, Cellular response, Concentration (process), Concentration of, Contact angle, controlled study, Cytokines, EGF, Electron energy levels, enzyme linked immunosorbent assay, Enzyme-Linked Immunosorbent Assay, epidermal growth factor, Epidermal growth factors, Ethylene, Glycols, gold, Gold substrates, human, human cell, Humans, Hydroxyl-terminated, Imidazoles, Immobilization process, Immobilization reaction, immunofluorescence, immunohistochemistry, Immunostaining, Molecular levels, Nanostructured materials, Nanostructured surface, Nanostructured surfaces, New model, Optimization, Phosphorylation, Photoelectron spectroscopy, Polyethylene Glycols, Protein adsorption, protein immobilization, protein interaction, protein phosphorylation, Proteins, Radiolabeling, Radioligand Assay, Reaction conditions, reaction optimization, Receptor, Epidermal Growth Factor, Sams, self assembled monolayer, Self assembled monolayers, Self-assembled monolayers, Sulfhydryl Compounds, Surface characterization, Surface functionalization, Surface models, Surface Properties, Water contact angle measurement, X ray photoelectron spectroscopy},
	isbn = {15493296 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-77953815323\&partnerID=40\&md5=7b54d717bbba475933dd86cc62659acc},
	author = {Gon{\c c}alves, R. and Martins, M.C.L. and Oliveira, M.J. and Almeida-Porada, G. and Barbosa, M.A.}
}
@article {2265,
	title = {Characterization of two DLC coatings for joint prosthesis: The role of albumin on the tribological behavior},
	journal = {Surface and Coatings TechnologySurf. Coat. Technol.},
	volume = {204},
	year = {2010},
	note = {Cited By (since 1996): 6Export Date: 21 November 2012Source: Scopusdoi: 10.1016/j.surfcoat.2010.04.022Language of Original Document: EnglishCorrespondence Address: Serro, A.P.; Centro de Qu{\'\i}mica Estrutural, Complexo I, Instituto Superior T{\'e}cnico, Av. Rovisco Pais, TU Lisbon, 1049-001 Lisboa, Portugal; email: anapaula.serro@ist.utl.ptReferences: Donnet, C., Erdemir, A., (2009), Springer Science \& Business Media, New YorkGutensohn, K., Beythien, C., Bau, J., Fenner, T., Grewe, P., Koester, R., Padmanaban, K., Kuehnl, P., (2000) Thromb. Res., 99, p. 577;Cadosch, D., Chan, E., Gautschi, O.P., Simmen, H.-P., Filgueira, L., (2009) J. Orthop. Res., 27, p. 841; 
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},
	month = {2010///},
	pages = {3451 - 3458},
	abstract = {A commonly used strategy for reduction of wear and friction of the sliding surfaces in prosthetic pairs is the use of hard coatings. DLCs (diamond like carbons) offer a promising solution, because these coatings, already used in other biomedical applications, exhibit a unique combination of chemical inertness, mechanical and tribological properties. In the present work we investigated the role of albumin, the most abundant protein in the periprosthetic fluid, on the tribological behavior of two DLCs with different compositions, against ultra-high molecular weight polyethylene (UHMWPE). The results are compared with those obtained with uncoated stainless steel surfaces. We have characterized the coatings by atomic force microscopy, X-ray diffraction, Raman spectroscopy, ultramicrohardness and wettability measurements. The adsorption of albumin onto the surfaces was investigated by ellipsometry and using a quartz crystal microbalance. Both DLCs adsorb a larger amount of protein than stainless steel. The tribological tests were performed in microtribometer aiming for a deeper understanding of the tribological mechanisms which occur at the submicrometric contact scale. Results showed no significant differences between the tribological behavior of the two coatings. Under the tested conditions, the tribological performance does not improve significantly with the application of the DLCs. Moreover, the presence of albumin on the lubricant leads to higher friction of the polymer against all counterfaces. This effect was attributed to the formation of bridges between the two sliding surfaces by the denaturated protein. The significant differences in the adsorbed amounts of protein onto the stainless steel and the two types of DLCs did not affect considerably the tribological behavior of these materials. {\textcopyright} 2010 Elsevier B.V.},
	keywords = {Adsorbed amount, Adsorption, Albumin adsorption, Atomic force microscopy, Atomic spectroscopy, Biomedical applications, Chemical inertness, Corrosion resistant alloys, Diamond like carbon, DLC coatings, Friction, Hard coatings, Joint prostheses, Mechanical and tribological properties, Mechanical properties, Microtribology, Microtribometer, Nonmetallic matrix composites, Oxide minerals, Polyethylenes, Proteins, Quartz, Raman spectroscopy, Scanning electron microscopy, Sliding surface, Stainless steel, Stainless steel surface, Steel corrosion, Surfaces, Tribological behaviors, Tribological mechanism, Tribological performance, Tribological tests, Tribology, UHMW-PE, UHMWPE, Ultramicrohardness, Wear and friction, Wettability measurements, X ray diffraction},
	isbn = {02578972 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-77953715334\&partnerID=40\&md5=d724bda7404d809fed9bafb6a5a337e3},
	author = {Carapeto, A.P. and Serro, A.P. and Nunes, B.M.F. and Martins, M.C.L. and Todorovic, S. and Duarte, M.T. and Andr{\'e}, V. and Cola{\c c}o, R. and Saramago, B.}
}
@article {2244,
	title = {Chitosan-based gene delivery vectors targeted to the peripheral nervous system},
	journal = {Journal of Biomedical Materials Research - Part AJ. Biomed. Mater. Res. Part A},
	volume = {95},
	year = {2010},
	note = {Cited By (since 1996): 5Export Date: 21 November 2012Source: ScopusCODEN: JBMRCdoi: 10.1002/jbm.a.32874PubMed ID: 20734332Language of Original Document: EnglishCorrespondence Address: P{\^e}go, A. P.; INEB, Instituto de Engenharia Biom{\'e}dica, Universidade Do Porto, Rua do Campo Alegre, 823, 4150-180 Porto, Portugal; email: apego@ineb.up.ptChemicals/CAS: DNA, 9007-49-2; chitosan, 9012-76-4; imidazole, 1467-16-9, 288-32-4; macrogol, 25322-68-3; Cations; Chitosan, 9012-76-4; DNA, 9007-49-2; Polyethylene GlycolsTradenames: Chimarin, medicarb, SwedenManufacturers: medicarb, SwedenReferences: Rodriguez, F.J., Valero-Cabre, A., Navarro, X., Regeneration and functional recovery following peripheral nerve injury (2004) Drug Discov Today, 1, pp. 177-185;Apfel, S.C., Neurotrophic factors in peripheral neuropathies: Therapeutic implications (1999) Brain Pathol, 9, pp. 393-413; 
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},
	month = {2010///},
	pages = {801 - 810},
	abstract = {A non-toxic, targeted, simple and efficient system that can specifically transfect peripheral sensorial neurons can pave the way towards the development of new therapeutics for the treatment of peripheral neuropathies. In this study chitosan (CH), a biodegradable polymer, was used as the starting material in the design of a multicomponent vector targeted to the peripheral nervous system (PNS). Polycation-DNA complexes were optimized using imidazole-and thiol-grafted CH (CHimiSH), in order to increase transfection efficiency and allow the formation of ligand conjugated nanocomplexes, respectively. The 50 kDa non-toxic fragment from the tetanus toxin (HC), shown to interact specifically with peripheral neurons and undergo retrograde transport, was grafted to the binary complex via a bi-functional poly(ethylene glycol) (HC-PEG) reactive for the thiol moieties present in the complex surface. The targeting of the developed nanocomplexes was assessed by means of internalization and transfection studies in the ND7/23 (neuronal) vs. NIH 3T3 (fibroblast) cell lines. Targeted transfection was further confirmed in dorsal root ganglion dissociated primary cultures. A versatile, multi-component nanoparticle system that successfully targets and transfects neuronal cell lines, as well as dorsal root ganglia (DRG) primary neuron cultures was obtained for the 1.0 (w/w) HC-PEG/DNA formulation. {\textcopyright} 2010 Wiley Periodicals, Inc.},
	keywords = {animal cell, Animals, article, Binary complexes, Biodegradable polymers, Carbohydrate Conformation, Carbohydrate Sequence, Cations, Cell culture, Cell lines, cell population, Cells, Cultured, Chitin, chitosan, Complex surface, DNA, DNA complex, Dorsal root ganglia, Efficient systems, embryo, Ethylene, Ethylene Glycol, Female, Ganglia, Spinal, Gene delivery, gene delivery system, Gene delivery vectors, Gene therapy, Gene transfer, Gene Transfer Techniques, genetic transfection, Genetic Vectors, Grafting (chemical), Humans, imidazole, macrogol, materials testing, Mice, Molecular Sequence Data, Molecular Structure, mouse, Multicomponents, Nanocomplexes, Nanoparticle systems, nanoparticles, nerve cell culture, Neuron culture, Neuronal cell, NIH 3T3 Cells, nonhuman, Nontoxic fragment of tetanus toxin, Peripheral nervous system, Peripheral neuropathy, Polycations, Polyethylene Glycols, Polyethylene oxides, Pregnancy, Primary culture, rat, Rats, Rats, Wistar, spinal ganglion, Starting materials, Targeted, Tetanus toxin, Toxic materials, Transfection, Transfection efficiency},
	isbn = {15493296 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-78249240032\&partnerID=40\&md5=af9c3ca5ca712d53abb5e80f45ed09c0},
	author = {Oliveira, H. and Pires, L.R. and Fernandez, R. and Martins, M.C.L. and Sim{\~o}es, S. and P{\^e}go, A.P.}
}
@article {2279,
	title = {The effect of immobilization of thrombin inhibitors onto self-assembled monolayers on the adsorption and activity of thrombin},
	journal = {BiomaterialsBiomaterials},
	volume = {31},
	year = {2010},
	note = {Cited By (since 1996): 7Export Date: 21 November 2012Source: ScopusCODEN: BIMADdoi: 10.1016/j.biomaterials.2010.01.097PubMed ID: 20153046Language of Original Document: EnglishCorrespondence Address: Martins, M.C.L.; INEB - Instituto de Engenharia Biom{\'e}dica, Divis{\~a}o de Biomateriais, Universidade do Porto, Rua do Campo Alegre 823, 4150-180 Porto, Portugal; email: cmartins@ineb.up.ptChemicals/CAS: thrombin, 9002-04-4; Albumins; Gold, 7440-57-5; Immobilized Proteins; Iodine Radioisotopes; Peptides; Solutions; Thrombin, 3.4.21.5References: Gorbet, M.B., Sefton, M.V., Biomaterial-associated thrombosis: roles of coagulation factors, complement, platelets and leukocytes (2004) Biomaterials, 25 (26), pp. 5681-5703;Ratner, B.D., Hoffman, A.F., Schoen, F.J., Lemons, J.L., (2004) Biomaterials science - an introduction to materials in medicine. 2nd ed., , Elsevier Academic Press, San Diego, CA, USA; 
Bode, W., Structure and interaction modes of thrombin (2006) Blood Cells Mol Dis, 36 (2), pp. 122-130; 
Huntington, J.A., Molecular recognition mechanisms of thrombin (2005) J Thromb Haemost, 3 (8), pp. 1861-1872; 
Schwienhorst, A., Direct thrombin inhibitors - a survey of recent developments (2006) Cell Mol Life Sci, 63 (23), pp. 2773-2791; 
Tseng, P.-Y., Rele, S.S., Sun, X.-L., Chaikof, E.L., Membrane-mimetic films containing thrombomodulin and heparin inhibit tissue factor-induced thrombin generation in a flow model (2006) Biomaterials, 27 (12), pp. 2637-2650; 
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Martins, M.C.L., Curtin, S.A., Freitas, S.C., Salgueiro, P., Ratner, B.D., Barbosa, M.A., Molecularly designed surfaces for blood deheparinization using an immobilized heparin-binding peptide (2009) J Biomed Mater Res A, 88 (1), pp. 162-173; 
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Martins, M.C.L., Naeemi, E., Ratner, B.D., Barbosa, M.A., Albumin adsorption on Cibacron Blue F3G-A immobilized onto oligo(ethylene glycol)- terminated self-assembled monolayers (2003) J Mater Sci Mater Med, 14 (11), pp. 945-954; 
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},
	month = {2010///},
	pages = {3772 - 3780},
	abstract = {Thrombus formation is the major problem associated with biomaterials for blood contact medical devices. The immobilization of inhibitors to thrombin, a serine protease that plays a central role on the coagulation system, on the surface of biomaterials should be a good strategy to avoid blood clotting and increase their hemocompatibility. The aim of this work is the design of a nanostructured surface with capacity to adsorb and inactivate thrombin. The pentapeptide sequence d-Phenylalanine-Proline-Arginine-Proline-Glycine (fPRPG), that was described as a thrombin inhibitor, was immobilized onto tetra(ethylene glycol) terminated self-assembled monolayers (EG4-SAMs). Surface containing different amounts of fPRPG were prepared using different concentrations of N,N'-Carbonyldiimidazole (CDI) during immobilization. The efficiency of fPRPG immobilization was followed using ellipsometry, contact angle measurements, Infrared reflection absorption spectroscopy (IRRAS) and X-ray photoelectron spectroscopy (XPS). Thrombin adsorption was quantified using radiolabelled thrombin and its activity in solution and after adsorption on the developed surfaces was assessed using a chromogenic assay. It was found that, although the immobilization of fPRPG on to EG4-SAMs does not increase its selectivity to thrombin, the activity of the adsorbed thrombin was inhibited in a peptide concentration dependent way. We concluded that SAMs with fPRPG immobilized in high amounts can be used as thrombin-inhibitor surfaces, which is a good step on the development of new surfaces for blood contact devices. {\textcopyright} 2010 Elsevier Ltd. All rights reserved.},
	keywords = {Absorption spectroscopy, Adsorption, adsorption kinetics, Albumins, Amino Acid Sequence, Amino acids, Angle measurement, article, Biomaterials, Blood, Blood clotting, Blood contact, Carbonyldiimidazole, Coagulation, Coagulation system, concentration (parameters), Concentration-dependent, Contact angle, D-phenylalanine, ellipsometry, Ethylene, Ethylene Glycol, ethylene glycol derivative, gold, Hemocompatibility, Humans, imidazole derivative, Immobilized Proteins, Infrared reflection absorption spectroscopy, infrared spectroscopy, Iodine Radioisotopes, isotope labeling, Medical Devices, monolayer culture, nanoanalysis, Nanostructured surface, peptide, Peptide immobilization, Peptides, phenylalanylprolylarginylprolylglycine, Phosphatases, priority journal, Protein adsorption, protein assembly, protein function, protein immobilization, quantitative study, Sams, Self assembled monolayers, Self-assembled monolayers, Serine protease, Solubility, Solutions, Spectroscopy, Fourier Transform Infrared, Surface functionalization, Surface Properties, Tetra, tetra(ethylene glycol), Thrombin, thrombin inhibitor, Thrombin inhibitors, Thrombus formation, unclassified drug, X ray photoelectron spectroscopy},
	isbn = {01429612 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-77649271932\&partnerID=40\&md5=f7180daf23d326319cf6d8dbf0eac77c},
	author = {Freitas, S.C. and Barbosa, M.A. and Martins, M.C.L.}
}
@article {2255,
	title = {The stability of self-assembled monolayers with time and under biological conditions},
	journal = {Journal of Biomedical Materials Research - Part AJ. Biomed. Mater. Res. Part A},
	volume = {94},
	year = {2010},
	note = {Cited By (since 1996): 7Export Date: 21 November 2012Source: ScopusCODEN: JBMRCdoi: 10.1002/jbm.a.32746PubMed ID: 20336761Language of Original Document: EnglishCorrespondence Address: Barbosa, M. A.; Divis{\~a}o de Biomateriais, INEB - Instituto de Engenharia Biom{\'e}dica, Universidade do Porto, Rua do Campo Alegre 823, Porto 4150-180, Portugal; email: mbarbosa@ineb.up.ptChemicals/CAS: sulfur, 13981-57-2, 7704-34-9; Culture Media; Ethanol, 64-17-5; Sulfhydryl Compounds; Sulfur, 7704-34-9; Water, 7732-18-5References: Mrksich, M., Whitesides, G.M., Using self-assembled monolayers to understand the interactions of man- Made surfaces with proteins and cells (1996) Annual Review of Biophysics and Biomolecular Structure, 25, pp. 55-78;Mrksich, M., Dike, L.E., Tien, J., Ingber, D.E., Whitesides, G.M., Using microcontact printing to pattern the attachment of mammalian cells to self-assembled monolayers of alkanethiolates on transparent films of gold and silver (1997) Exp Cell Res, 235, pp. 305-313; 
Flynn, N.T., Tran, T.N.T., Cima, M.J., Langer, R., Long-term stability of self-assembled monolayers in biological media (2003) Langmuir, 19, pp. 10909-10915; 
Willey, T.M., Vance, A.L., Van Buuren, T., Bostedt, C., Terminello, L.J., Fadley, C.S., Rapid degradation of alkanethiol-based self-assembled monolayers on gold in ambient laboratory conditions (2005) Surf Sci, 576, pp. 188-196; 
Jones, J.A., Qin, L.A., Meyerson, H., Kwon, I.K., Matsuda, T., Anderson, J.M., Instability of self-assembled monolayers as a model material system for macrophage/FBGC cellular behavior (2008) J Biomed Mater Res Part A, 86 A, pp. 261-268; 
Martins, M.C.L., Ratner, B.D., Barbosa, M.A., Protein adsorption on mixtures of hydroxyl- And methyl-terminated alkanethiols self-assembled monolayers (2003) Journal of Biomedical Materials Research - Part a, 67 (1), pp. 158-171; 
Martins, M.C.L., Fonseca, C., Barbosa, M.A., Ratner, B.D., Albumin adsorption on alkanethiols self-assembled monolayers on gold electrodes studied by chronopotentiometry (2003) Biomaterials, 24, pp. 3697-3706; 
Bain, C.D., Troughton, E.B., Tao, Y.T., Evall, J., Whitesides, G.M., Nuzzo, R.G., Formation of monolayer films by the spontaneous assembly of organic thiols from solution onto gold (1989) J Am Chem Soc, 111, pp. 321-335; 
Sastry, M., A note on the use of ellipsometry for studying the kinetics of formation of self-assembled monolayers (2000) Bull Mater Sci, 23, pp. 159-163; 
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Rodrigues, S.N., Goncalves, I.C., Martins, M.C.L., Barbosa, M.A., Ratner, B.D., Fibrinogen adsorption, platelet adhesion and activation on mixed hydroxyl-/methyl-terminated self-assembled monolayers (2006) Biomaterials, 27, pp. 5357-5367; 
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Martins, M.C.L., Curtin, S.A., Freitas, S.C., Salgueiro, P., Ratner, B.D., Barbosa, M.A., Molecularly designed surfaces for blood deheparinization using an immobilized heparin-binding peptide (2009) J Biomed Mater Res Part A, 88 A, pp. 162-173; 
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},
	month = {2010///},
	pages = {833 - 843},
	abstract = {The stability of self-assembled monolayers (SAMs) of different functionalities (CH                        3
},
	keywords = {Animals, article, Binding energy, Biological conditions, Biological studies, Body fluids, Cattle, Cell culture, Culture Media, Ethanol, Female, Fetal bovine serum, In-cell, materials testing, measurement, molecular stability, Nitrogen chamber, nonhuman, Organic polymers, Oxidation, Oxidation-Reduction, Oxidized sulfur, Photodegradation, Photoelectron spectroscopy, Sams, self assembled monolayer, Self assembled monolayers, Self-assembled monolayers, Stability, Storage condition, Sulfhydryl Compounds, Sulfur, Surface Properties, Water, wettability, X ray photoelectron spectroscopy, XPS, XPS spectra},
	isbn = {15493296 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-77954806701\&partnerID=40\&md5=9c561e8b43c045cdeb8d80a42148c6ca},
	author = {Maciel, J. and Martins, M.C.L. and Barbosa, M.A.}
}
@article {2275,
	title = {Targeted gene delivery into peripheral sensorial neurons mediated by self-assembled vectors composed of poly(ethylene imine) and tetanus toxin fragment c},
	journal = {Journal of Controlled ReleaseJ. Control. Release},
	volume = {143},
	year = {2010},
	note = {Cited By (since 1996): 13Export Date: 21 November 2012Source: ScopusCODEN: JCREEdoi: 10.1016/j.jconrel.2010.01.018PubMed ID: 20093157Language of Original Document: EnglishCorrespondence Address: P{\^e}go, A.P.; INEB-Instituto de Engenharia Biom{\'e}dica, Divis{\~a}o de Biomateriais, Universidade do Porto, Rua do Campo Alegre, 823, 4150-180 Porto, Portugal; email: apego@ineb.up.ptChemicals/CAS: DNA, 9007-49-2; macrogol, 25322-68-3; polyethyleneimine, 74913-72-7; DNA, 9007-49-2; Imines; Peptide Fragments; Polyethylenes; Tetanus Toxin; poly(ethylene imine); tetanus toxin fragment CReferences: Rodriguez, F.J., Valero-Cabre, A., Navarro, X., Regeneration and functional recovery following peripheral nerve injury (2004) Drug Discov. Today, 1 (2), pp. 177-185;Sahenk, Z., Neurotrophins and peripheral neuropathies (2006) Brain Pathol., 16 (4), pp. 311-319; 
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},
	month = {2010///},
	pages = {350 - 358},
	abstract = {A simple, safe and efficient system that can specifically transfect peripheral sensorial neurons can bring new answers to address peripheral neuropathies. A multi-component non-viral gene delivery vector targeted to peripheral nervous system cells was developed, using poly(ethylene imine) (PEI) as starting material. A binary DNA/polymer complex based on thiolated PEI (PEISH) was optimized, considering complex size and zeta potential and the ability to transfect a sensorial neuron cell line (ND7/23). The 50. kDa non-toxic fragment from tetanus toxin (HC), which has been previously shown to interact specifically with peripheral neurons and to undergo retrograde transport, was grafted to the complex core via a bifunctional PEG (HC-PEG) reactive for the thiol moieties present in the complex surface. Several formulations of HC-PEG ternary complexes were tested for targeting, by assessing the extent of cellular internalization and levels of transfection, in both the ND7/23 and NIH 3 T3 (fibroblast) cell lines. Targeted gene transfer to the neuronal cell line was observed for the complex formulations containing 5 and 7.5. Μg of HC-PEG. Finally, our results demonstrate that the developed ternary vectors are able to transfect primary cultures of dorsal root ganglion dissociated neurons in a targeted manner and elicit the expression of a relevant neurotrophic factor. {\textcopyright} 2010 Elsevier B.V.},
	keywords = {Aberrations, animal cell, Animals, article, Bifunctional, Cell culture, Cell Line, Tumor, Cell lines, cell strain 3T3, Cells, Cultured, Cellular internalization, Chemical modification, Complex cores, Complex formulations, Complex surface, controlled study, DNA, DNA protein complex, Dorsal root ganglia, Efficient systems, embryo, Ethylene, Female, Gene transfer, genetic transfection, Imines, internalization, macrogol, Mice, mouse, Multicomponents, nanoparticle, nanoparticles, neuroblastoma cell, Neuronal cell, Neurons, neurotrophic factor, Neurotrophic factors, NIH 3T3 Cells, Nitrogen compounds, Non-viral, Non-viral gene delivery, nonhuman, Nonviral, nonviral gene delivery system, Nucleic acids, Particle Size, Peptide Fragments, Peripheral nervous system, Peripheral neuropathy, Plasmids, Polyethylene Glycols, Polyethylene oxides, Polyethyleneimine, Polyethylenes, Primary culture, priority journal, process optimization, protein expression, rat, Rats, Rats, Wistar, Regenerative Medicine, Self-assembled, sensory nerve cell, spinal ganglion, Starting materials, Targeted, Targeted gene delivery, Ternary complex, Ternary vectors, Tetanus toxin, tetanus toxin fragment c, Transfection, unclassified drug, Zeta potential},
	isbn = {01683659 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-77952239026\&partnerID=40\&md5=077b03d49cf392defc3d0c77f2f249d1},
	author = {Oliveira, H. and Fernandez, R. and Pires, L.R. and Martins, M.C.L. and Sim{\~o}es, S. and Barbosa, M.A. and P{\^e}go, A.P.}
}
@article {2323,
	title = {The correlation between the adsorption of adhesive proteins and cell behaviour on hydroxyl-methyl mixed self-assembled monolayers},
	journal = {BiomaterialsBiomaterials},
	volume = {30},
	year = {2009},
	note = {Cited By (since 1996): 41Export Date: 21 November 2012Source: ScopusCODEN: BIMADdoi: 10.1016/j.biomaterials.2008.09.048PubMed ID: 18952279Language of Original Document: EnglishCorrespondence Address: Barrias, C.C.; INEB - Instituto de Engenharia Biom{\'e}dica, Divis{\~a}o de Biomateriais, Universidade do Porto, R. Campo Alegre 823, 4150-180 Porto, Portugal; email: ccbarrias@ineb.up.ptChemicals/CAS: fibronectin, 86088-83-7; gold, 7440-57-5; thiol derivative, 13940-21-1; Biocompatible Materials; Fibronectins; VitronectinReferences: Wilson, C.J., Clegg, R.E., Leavesley, D.I., Pearcy, M.J., Mediation of biomaterial-cell interactions by adsorbed proteins: a review (2005) Tissue Eng, 11, pp. 1-18;Garc{\'\i}a, A.J., Vega, M.D., Boettiger, D., Modulation of cell proliferation and differentiation through substrate-dependent changes in fibronectin conformation (1999) Mol Biol Cell, 10, pp. 785-798; 
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},
	month = {2009///},
	pages = {307 - 316},
	abstract = {The objective of this study was to compare the biological effects of two key cell-adhesive proteins, fibronectin (FN) and vitronectin (VN), upon adsorption onto molecularly-designed model surfaces. Single-component and mixed self-assembled monolayers (SAMs) of alkanethiols on gold with OH and CH                        3 terminal groups were prepared at 100\%, 65\%, 36\% and 0\% of OH at the surface, to generate a range of surfaces with a simple chemistry and a wettability gradient. FN and VN were adsorbed under non-competitive (single-protein solutions) and competitive (multi-protein solutions) conditions, and compared at different levels: adsorbed amount (radiolabelling), elution, functional presentation of cell-binding domains (ELISA), and role in mediating cell adhesion (antibody-based assay). The observed trends were related to mesenchymal stem cell response in terms of adhesion and overall cell morphology. Under non-competitive conditions, adsorption of both proteins increased with surface hydrophobicity. The presence of competitive proteins significantly decreased the adsorbed amounts, although both proteins were still detected in all SAMs. Adsorption of FN followed a trend similar to that of non-competitive conditions, while adsorption of VN was higher on 100\%OH-SAMs. Concerning elution, retention of adsorbed VN was always higher than that of FN. For both proteins, functional presentation of cell-binding domains was more effective on the more hydrophilic 100\%OH-SAMs. This fact, coupled to the ability of this type of SAMs to selectively recruit and retain VN in the presence of competitive serum proteins, seems to correlate with the better cell response observed on these surfaces, as compared with hydrophobic 0\%OH(100\%CH
                        3)-SAMs. {\textcopyright} 2008 Elsevier Ltd. All rights reserved.
},
	keywords = {Adhesion, Adhesiveness, Adsorption, alkane, Animals, article, Biocompatible Materials, Biological Assay, bone marrow, Cattle, cell adhesion, Cell culture, Cell Movement, Cells, Cells, Cultured, cytology, cytoskeleton, Electric currents, Electron energy levels, enzyme linked immunosorbent assay, Fibronectin, Fibronectins, Focal adhesions, Functional groups, Functionalization, gold, human, human cell, Humans, hydrophilicity, hydrophobicity, Hydroxylation, isotope labeling, Mesenchymal stem cell, Mesenchymal Stem Cells, Microscopy, Confocal, Missile bases, Molecular interactions, monoclonal antibody, priority journal, Protein adsorption, protein analysis, protein binding, Protein Structure, Tertiary, Proteins, Self assembled monolayers, Self-assembled monolayers, stem cell, Stem cells, Surface Properties, thiol derivative, Vitronectin},
	isbn = {01429612 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-55249093830\&partnerID=40\&md5=132fa4efe300c4f76764942bfe3bce30},
	author = {Barrias, C.C. and Martins, M.C.L. and Almeida-Porada, G. and Barbosa, M.A. and Granja, P.L.}
}
@article {2291,
	title = {Induction of notch signaling by immobilization of jagged-1 on self-assembled monolayers},
	journal = {BiomaterialsBiomaterials},
	volume = {30},
	year = {2009},
	note = {Cited By (since 1996): 6Export Date: 21 November 2012Source: ScopusCODEN: BIMADdoi: 10.1016/j.biomaterials.2009.09.010PubMed ID: 19783294Language of Original Document: EnglishCorrespondence Address: Gon{\c c}alves, R.M.; INEB, Biomaterials Division, NEWTherapies Group, R. Campo Alegre, 823, 4150-180 Porto, Portugal; email: raquelg@ineb.up.ptChemicals/CAS: Calcium-Binding Proteins; Gold, 7440-57-5; Immunoglobulin G; Intercellular Signaling Peptides and Proteins; Membrane Proteins; Receptors, Fc; Receptors, Notch; Recombinant Fusion Proteins; Serrate proteins, 134324-36-0References: Artavanis-Tsakonas, S., Rand, M.D., Lake, R.J., Notch signaling: cell fate control and signal integration in development (1999) Science, 284, pp. 770-776;Leong, K., Karsan, A., Recent insights in the role of notch signaling in tumorigenesis (2006) Blood, 107 (6), pp. 2223-2233; 
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Love, J., Estroff, L.A., Kriebel, J.K., Nuzzo, R.G., Whitesides, G.M., Self-assembled monolayers of thiolates on metals as a form of nanotechnology (2005) Chem Rev, 105, pp. 1103-1169; 
Gehanno, V., Freitas, P.P., Veloso, A., Ferreira, J., Almeida, B., Sousa, J.B., Ion beam deposition of Mn-Ir spin valves (1999) IEEE Trans Magn, 35, pp. 4361-4367; 
Martins, M.C.L., Ratner, B., Barbosa, M.A., Protein adsorption on mixtures of hydroxyl- and methyl- terminated self-assembled monolyers (2003) J Biomed Mater Res, 67 (A), pp. 158-171; 
Martins, M.C.L., Curtins, S.A., Freitas, S.C., Salgueiro, P., Ratner, B.D., Barbosa, M.A., Molecularly designed surfaces for blood deheparinization using an immobilized heparin-binding peptide (2009) J Biomed Mater Res A, 88 (1), pp. 162-173; 
Barrias, C.C., Martins, M.C.L., Bidarra, S., S{\'a} Miranda, M.C., Barbosa, M.A., Adsorption of a therapeutic enzyme to self-assembled monolayers: effect of the surface chemistry and solution pH on the amount and activity of adsorbed enzyme (2005) Biomaterials, 26, pp. 2695-2704; 
Iodine-125. A guide to radioiodination techniques. In: techniques I-Agtr, ed.: Little Chalfort: Amersham Life Science 1993Horbett, T., Techniques for protein adsorption studies (1986) Techniques of biocompatibility tests, pp. 183-214. , DF W. (Ed), CRC Press Inc, Harcover; 
Ohishi, K., Varnum-Finney, B., Bernstein, I.D., Delta-1 enhances marrow and thymus repopulating ability of human CD34+ CD38- cord blood cells (2002) J Clin Invest, 110, pp. 1165-1174; 
Li, L., Chen, S., Zheng, J., Ratner, B.D., Jiang, S., Protein adsorption on oligo(ethylene glycol)-terminated alkanethiolate self-assembled monolayers: the molecular basis for nonfouling behavior (2005) J Phys Chem B, 109 (7), pp. 2934-2941; 
Tohda, S., Murata-Ohsawa, M., Sakano, S., Nara, N., Notch ligands, Delta-1 and Delta-4 supress the self-renewal capacity and long-term growth of two myeloblastic leukemia cell lines (2003) Int J Oncol, 22 (5), pp. 1073-1079; 
Tohda, S.K.H., Murakami, N., Sakano, S., Nara, N., Diverse effects of the Notch ligands Jagged1 and Delta1 on the growth and differentiation of primary acute myeloblastic leukemia cells (2005) Exp Hematol, 33, pp. 558-563; 
Aoyama, K., Delaney, C., Varnun-Finney, B., Kohn, A.D., Moon, R.T., Bernstein, I.D., The interaction of the Wnt and notch pathways modulates natural killer versus T cell differentiation (2007) Stem Cells, 25, pp. 2488-2497; 
Beckstead B, Tung JC, Liang KJ, Tavakkol Z, Usui ML, Olerud JE, et~al. Methods to promote notch signaling at the biomaterial interface and evaluation in a rafted organ culture model. J Biomed Mater Res A, in press. [Epub ahead of print]Semler, E., Dasgupta, A., Moghe, P.V., Cytomimetic engineering of hepatocyte morphogenesis and function by substrate-based presentation of acellular E-cadherin (2005) Tissue Eng, 11 (5-6), pp. 734-750; 
Zhao, Z., Matsui, H., Accurate immobilization of antibody-functionalized peptide nanotubes on protein-patterned arrays by optimizing their ligand-receptor interactions (2007) Small, 3 (8), pp. 1390-1393; 
Longo, G., Szleifer, Ligand-receptor interactions in tethered polymer layers (2005) Langmuir, 21, pp. 11342-11351; 
Gon{\c c}alves, I.C., Martins, M.C.L., Barbosa, M.A., Ratner, B.D., Protein adsorption and clotting time of pHEMA hydrogels modified with C18 ligands to adsorb albumin selectively and reversibly (2009) Biomaterials, 30 (29), pp. 5541-5551
},
	month = {2009///},
	pages = {6879 - 6887},
	abstract = {Notch signaling is a key mechanism during mammal development and stem cell regulation. This study aims to target and control Notch signaling by ligands immobilization using self-assembled monolayers (SAMs) as model surfaces. Non-fouling substrates were prepared by immersion of gold substrates in (1-Mercapto-11-undecyl)tetra(ethylene glycol) thiol solutions. These surfaces were activated with N,N'-carbonyldiimidazole (CDI) at different concentrations (0, 0.03, 0.3, 3 and 30 mg/ml) and an anti-human IgG, Fc specific fragment antibody (Ab) was covalently bound to EG4-SAMs to guarantee the correct exposure of the Notch ligand Jagged-1/Fc chimera (Jag-1). The presence of Ab and Jag-1 was confirmed by radiolabeling, X-ray photoelectron spectroscopy (XPS), ellipsometry and ELISA. The biological activity of Jag-1-Ab-SAMs was assessed by real-time PCR for Hes-1 family gene expression, a Notch pathway target gene, in HL-60 cell line. Results have shown an increase of the amount of immobilized Ab with increasing surface activator concentrations. Jag-1 concentration also increases with Ab concentration. Interestingly, a higher Jagged-1 exposure and fold increase in Hes-1 expression were obtained for surfaces activated with the lowest concentration of CDI (0.03 mg/ml). These results illustrate the great importance of ligands orientation and exposure, when compared with density. This investigation brings new insights into Notch signaling mechanisms. In particular, Jag-1-Ab-SAMs have shown to be adequate model surfaces to study Notch pathway activation and may provide a basis to develop new interfaces in biomaterials to control Notch mechanism in different cell systems. {\textcopyright} 2009 Elsevier Ltd.},
	keywords = {Activator concentration, Adequate models, Adsorption, Animals, article, Bioactivity, Biological activities, Biological materials, biomaterial, Calcium-Binding Proteins, Carbonyldiimidazole, Cell culture, Cell Line, Cell membranes, cell strain HL 60, Cell system, Chemical activation, Concentration (process), Concentration of, controlled study, Covalently bound, Ethylene, Ethylene Glycol, gene expression, gold, Gold substrates, HL-60 cell line, human, human cell, Human IgG, Humans, Immunoassay, immunoglobulin Fc fragment, Immunoglobulin G, immunoglobulin G antibody, Intercellular Signaling Peptides and Proteins, Jagged1, Ligands, Mammalia, Membrane Proteins, Model surface, Molecular Structure, Nanostructured materials, Nanostructured surfaces, Nonfouling, Notch receptor, Notch signaling, Photoelectron spectroscopy, priority journal, Protein adsorption, protein immobilization, Radiolabeling, Real-time PCR, Receptors, Fc, Receptors, Notch, Recombinant Fusion Proteins, Sams, self assembled monolayer, Self assembled monolayers, Self-assembled monolayers, signal transduction, Signaling, stem cell, Surface Properties, Target genes, Tetra, transcription factor HES 1, X ray photoelectron spectroscopy},
	isbn = {01429612 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-70350188310\&partnerID=40\&md5=6c55d29cf8ae55288f3e87880171ec70},
	author = {Gon{\c c}alves, R.M. and Martins, M.C.L. and Almeida-Porada, G. and Barbosa, M.A.}
}
@article {2325,
	title = {Molecularly designed surfaces for blood deheparinization using an immobilized heparin-binding peptide},
	journal = {Journal of Biomedical Materials Research - Part AJ. Biomed. Mater. Res. Part A},
	volume = {88},
	year = {2009},
	note = {Cited By (since 1996): 12Export Date: 21 November 2012Source: ScopusCODEN: JBMRCdoi: 10.1002/jbm.a.31849PubMed ID: 18286636Language of Original Document: EnglishCorrespondence Address: Martins, M. C. L.; INEB - Instituto de Engenharia Biom{\'e}dica, Divis{\~a}o de Biomaterials, Universidade do Porto, Rua do Campo Alegre, 823, 4150-180, Porto, Portugal; email: cmartins@ineb.up.ptChemicals/CAS: carbonyldiimidazole, 530-62-1; heparin, 37187-54-5, 8057-48-5, 8065-01-8, 9005-48-5; imidazole, 1467-16-9, 288-32-4; leucine, 61-90-5, 7005-03-0; lysine, 56-87-1, 6899-06-5, 70-54-2; tetraethylene glycol, 112-60-7; Ethylene Glycol, 107-21-1; Heparin, 9005-49-6; Leucine, 61-90-5; Lysine, 56-87-1; PeptidesReferences: Dailey J. Blood. Ipswich, MA, USA: Medical Consulting Group; 1998Section, V., Chronic intermittent haemodialysis and prevention of clotting in the extracorporal system (2002) Nephrol Dialysis Transplant, 17, pp. 63-71;Zhang, Y.H., Singh, V.K., Yang, V.C., Novel approach for optimizing the capacity and efficacy of a protamine filter for clinical extracorporeal heparin removal (1998) Asaio J, 44, pp. M368-M373; 
Tao, W., Deyo, D.J., Brunston, R.L., Vertrees, R.A., Zwischenberger, J.B., Extracorporeal heparin adsorption following cardiopulmonary bypass with a heparin removal device - An alternative to protamine (1998) Critical Care Med, 26, pp. 1096-1102; 
Ameer, G.A., Barabino, G., Sasisekharan, R., Harmon, W., Cooney, C.L., Langer, R., Ex vivo evaluation of a Taylor-Couette flow, immobilized heparinase I device for clinical application (1999) Proc Natl Acad Sci USA, 96, pp. 2350-2355; 
Ostuni, E., Yan, L., Whitesides, G.M., The interaction of proteins and cells with self-assembled monolayers of alkanethiolates on gold and silver (1999) Colloids Surf B-Biointerfaces, 15, pp. 3-30; 
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Kricheldorf, H.R., (1987) α-Amino Acid N-Carboxyanhydrides and Related Heterocycles, , New York: Springer Verlag;; 
Martins, M.C.L., Ratner, B.D., Barbosa, M.A., Protein adsorption on mixtures of hydroxyl- and methylterminated alkanethiols self-assembled monolayers (2003) J Biomed Mater Res A, 67, pp. 158-171; 
Lee, H.J., Nedelkov, D., Corn, R.M., Surface plasmon resonance imaging measurements of antibody arrays for the multiplexed detection of low molecular weight protein biomarkers (2006) Anal Chem, 78, pp. 6504-6510; 
Roeges, N.P.G., (1994) A Guide to the Complete Interpretation of Infrared Spectra of Organic Structures, , England: Wiley;; 
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Beamson, G., High, B.D., (1992) Resolution XPS of Organic Polymers, , Chichester: Wiley;; 
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Socrates, G., (2001) Infrared and Raman Characteristic Group Frequencies: Tables and Charts, , Chichester: Wiley;; 
Capila, I., Linhardt, R.J., Heparin - Protein interactions (2002) Angewandte Chemie-Int Ed, 41, pp. 391-112; 
Snell, C.R.F.G., Kinetics and thermodynamics of the alpha Helix - β Transconformation of poly(L-lysine) and L-leucine copolymers. A compensation phenomenon (1973) Biochemistry, 12, pp. 1017-1025; 
Hearn, M.T.W., 1,1'-Carbonyldiimidazole-mediated immobilization of enzymes and affinity ligands (1987) Methods Enzymol, 135, pp. 102-117; 
Stollner, D., Scheller, F.W., Warsinke, A., Activation of cellulose membranes with 1,1'-carbonyldiimidazole or 1-cyano-4-dimethylaminopyridinium tetrafluoroborate as a basis for the development of immunosensors (2002) Anal Biochem, 304, pp. 157-165
},
	month = {2009///},
	pages = {162 - 173},
	abstract = {Systemic heparinization, used during haemodialysis to prevent blood clotting on the extracorporeal circuit, leads to a high incidence of hemorrhagic complications. The adverse reactions associated with heparin neutralization using protamine sulphate justify the development of an alternative system for blood deheparinization. The main objective of this work is to design nanostructured surfaces with the capacity to bind heparin from blood in a selective way. A heparin-binding polypeptide, composed of L-lysine and L-leucine (pKL), was synthesized and immobilized, in different concentrations, onto self-assembled monolayers (SAMs) terminated with tetra(ethylene-glycol) (EG4 SAMs). Immobilization was performed using a fixed concentration of pKL after surface activation to different degrees using a range of CDI (N,N'-carbonyldiimidazole) concentrations. Results demonstrated that the presence of pKL increases heparin adsorption to EG4-SAMs, independently of the pKL concentration and the way of immobilization (adsorption or covalent bound). Selectivity towards heparin was successfully achieved on SAMs with low concentrations of immobilized pKL (9-17\% of pKL). Surfaces were characterized using ellipsometry, contact angle measurements, Fourier transform infrared reflection absorption spectroscopy (IRAS), atomic force microscopy, and X-ray photoelectron spectroscopy. Heparin adsorption was assessed using IRAS and N-sulphonate-                        35S-heparin. Therefore, this study could give a good contribution for the design of blood deheparinization devices. {\textcopyright} 2008 Wiley Periodicals, Inc.
},
	keywords = {Absorption spectroscopy, Adsorption, Alternative systems, Amines, Amino acids, Angle measurement, article, Atomic force microscopy, Atomic forces, Atomic spectroscopy, Binding peptides, Blood, Blood clotting, Carbonyl diimidazole, Carbonyldiimidazole, Contact angle, deheparinization, device, Dialysis, Electron energy levels, ellipsometry, Ethylene, Ethylene Glycol, Fourier Transform Infrared, Fourier transforms, Glycols, Haemodialysis, heparin, heparin binding protein, Heparinization, High incidences, Humans, imidazole, immobilization, infrared spectroscopy, leucine, Low concentrations, lysine, Methods, Missile bases, Monolayers, nanomaterial, Nanostructured surfaces, Nanostructures, Peptide immobilization, Peptides, Photoelectron spectroscopy, Polysaccharides, Protein adsorption, protein binding, Renal Dialysis, Self assembled monolayers, Self-assembled monolayers, Sulphate, Surface activations, Surface functionalization, Surface Properties, surface property, tetraethylene glycol, unclassified drug, X ray photoelectron spectroscopy, X-ray photoelectron spectroscopies},
	isbn = {15493296 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-57449118932\&partnerID=40\&md5=8f442ccbde0273f4ed4e04024a75fd37},
	author = {Martins, M.C.L. and Curtin, S.A. and Freitas, S.C. and Salgueiro, P. and Ratner, B.D. and Barbosa, M.A.}
}
@article {2298,
	title = {Protein adsorption and clotting time of pHEMA hydrogels modified with C18 ligands to adsorb albumin selectively and reversibly},
	journal = {BiomaterialsBiomaterials},
	volume = {30},
	year = {2009},
	note = {Cited By (since 1996): 9Export Date: 21 November 2012Source: ScopusCODEN: BIMADdoi: 10.1016/j.biomaterials.2009.06.025PubMed ID: 19595453Language of Original Document: EnglishCorrespondence Address: Gon{\c c}alves, I.C.; INEB - Instituto de Engenharia Biom{\'e}dica, Divis{\~a}o de Biomateriais, Universidade do Porto, Rua do Campo Alegre, 823, 4150-180 Porto, Portugal; email: icastro@ineb.up.ptChemicals/CAS: fibrinogen, 9001-32-5; human serum albumin, 9048-49-1; polymacon, 25053-81-0, 25249-16-5, 98932-78-6; polystyrene, 9003-53-6; Biocompatible Materials; Coated Materials, Biocompatible; Hydrogels; Polyhydroxyethyl Methacrylate, 25249-16-5; Serum AlbuminReferences: Kottkemarchant, K., Anderson, J.M., Umemura, Y., Marchant, R.E., Effect of albumin coating on the in vitro blood compatibility of dacron arterial prostheses (1989) Biomaterials, 10 (3), pp. 147-155;Ji, J., Feng, L.X., Barbosa, M.A., Stearyl poly(ethylene oxide) grafted surfaces for preferential adsorption of albumin (2001) Biomaterials, 22 (22), pp. 3015-3023; 
Keogh, J.R., Eaton, J.W., Albumin-binding surfaces for biomaterials (1994) The Journal of Laboratory and Clinical Medicine, 124 (4), pp. 537-545; 
Keogh, J.R., Velander, F.F., Eaton, J.W., Albumin-binding surfaces for implantable devices (1992) Journal of Biomedical Materials Research, 26 (4), pp. 441-456; 
Martins, M.C.L., Wang, D., Ji, J., Feng, L., Barbosa, M.A., Albumin and fibrinogen adsorption on Cibacron blue F3G-A immobilised onto PU-PHEMA (polyurethane-poly(hydroxyethylmethacrylate)) surfaces (2003) Journal of Biomaterials Science Polymer Edition, 14 (5), pp. 439-455; 
McFarland, C.D., De Filippis, C., Jenkins, M., Tunstell, A., Rhodes, N.P., Williams, D.F., Albumin-binding surfaces: in vitro activity (1998) Journal of Biomaterials Science Polymer Edition, 9 (11), pp. 1227-1239; 
Munro, M.S., Quattrone, A.J., Ellsworth, S.R., Kulkarni, P., Eberhart, R.C., Alkyl substituted polymers with enhanced albumin affinity (1981) Transactions American Society for Artificial Internal Organs, 27, pp. 499-503; 
Tsai, C.C., Huo, H.H., Kulkarni, P., Eberhart, R.C., Biocompatible coatings with high albumin affinity (1990) ASAIO Transactions, 36 (3), pp. 307-310; 
Wang, D.A., Chen, B.L., Ji, J., Feng, L.X., Selective adsorption of serum albumin on biomedical polyurethanes modified by a poly(ethylene oxide) coupling-polymer with Cibacron blue (F3G-A) endgroups (2002) Bioconjugate Chemistry, 13 (4), pp. 792-803; 
Gon{\c c}alves, I.C., Martins, M.C.L., Barbosa, M.A., Naeemi, E., Ratner, B.D., Selective protein adsorption modulates platelet adhesion and activation to oligo(ethylene glycol)-terminated self-assembled monolayers with C18 ligands (2009) Journal of Biomedical Materials Research Part A, 89 A (3), pp. 642-653; 
Bain, C.D., Troughton, E.B., Tao, Y.T., Evall, J., Whitesides, G.M., Nuzzo, R.G., Formation of monolayer films by the spontaneous assembly of organic thiols from solution onto gold (1989) Journal of the American Chemical Society, 111 (1), pp. 321-335; 
Kwok, S.C., Mourad, P.D., Crum, L.A., Ratner, B.D., Surface modification of polymers with self-assembled molecular structures: multitechnique surface characterization (2000) Biomacromolecules, 1, pp. 139-148; 
Goncalves, I.C., Martins, M.C.L., Barbosa, M.A., Ratner, B.D., Protein adsorption on 18-alkyl chains immobilized on hydroxyl-terminated self-assembled monolayers (2005) Biomaterials, 26 (18), pp. 3891-3899; 
Ratner, B.D., Hoffman, A.F., Schoen, F.J., Lemons, J.L., (2004) Biomaterials science - an introduction to materials in medicine. 2nd ed., , Elsevier Academic Press, San Diego, CA, USA; 
Ratner, B.D., Miller, I.F., Interaction of urea with poly(2-hydroxyethyl methacrylate) hydrogels (1972) Journal of Polymer Science Part a-1-Polymer Chemistry, 10 (8), pp. 2425-2445; 
Horbett, T.A., Techniques for protein adsorption studies (1986) Techniques of biocompatibility testing, pp. 183-214. , Williams D.F. (Ed), Harcover: CRC Press; 
Cao, L., Chang, M., Lee, C.Y., Castner, D.G., Sukavaneshvar, S., Ratner, B.D., Plasma-deposited tetraglyme surfaces greatly reduce total blood protein adsorption, contact activation, platelet adhesion, platelet procoagulant activity, and in vitro thrombus deposition (2007) Journal of Biomedical Materials Research Part A, 81 (4), pp. 827-837; 
Stovbun, E.V., Kuzaev, A.I., Baturin, S.M., (1996) Polymer Science Series A, 38, pp. 691-695; 
Tanaka, M., Motomura, T., Kawada, M., Anzai, T., Yuu, K., Shiroya, T., Blood compatible aspects of poly(2-methoxyethylacrylate) (PMEA) - relationship between protein adsorption and platelet adhesion on PMEA surface (2000) Biomaterials, 21 (14), pp. 1471-1481; 
Castner, D.G., Ratner, B.D., Hirao, A., Nakahama, S., Characterization of poly(2-hydroxyethyl methacrylate) (PHEMA) by XPS (1996) Surface Science Spectra, 4 (1-4), p. 14; 
L{\'o}pez, G.P., Ratner, B.D., Rapoza, R.J., Horbett, T.A., Plasma deposition of ultrathin films of poly(2-hydroxyethyl methacrylate): surface analysis and protein adsorption measurements (1993) Macromolecules, 26 (13), pp. 3247-3253; 
Martins, M.C.L., Wang, D., Ji, J., Feng, L., Barbosa, M.A., Albumin and fibrinogen adsorption on PU-PHEMA surfaces (2003) Biomaterials, 24 (12), pp. 2067-2076; 
Tsukagoshi, T., Kondo, Y., Yoshino, N., Protein adsorption on polymer-modified silica particle surface (2007) Colloids and Surfaces B Biointerfaces, 54 (1), pp. 101-107; 
Ratner, B.D., Biomedical applications of hydrogels: review and critical appraisal (1981) Biocompatibility of clinical implant materials, , Williams D.F. (Ed), CRC Press; 
H{\"o}{\"o}k, F., V{\"o}r{\"o}s, J., Rodahl, M., Kurrat, R., B{\"o}ni, P., Ramsden, J.J., A comparative study of protein adsorption on titanium oxide surfaces using in situ ellipsometry, optical waveguide lightmode spectroscopy, and quartz crystal microbalance/dissipation (2002) Colloids and Surfaces B Biointerfaces, 24 (2), pp. 155-170; 
Stryer, L., (1998) Biochemistry. 4th ed., , WH Freeman, New York; 
Garrett, Q., Chatelier, R.C., Griesser, H.J., Milthorpe, B.K., Effect of charged groups on the adsorption and penetration of proteins onto and into carboxymethylated poly(HEMA) hydrogels (1998) Biomaterials, 19 (23), pp. 2175-2186; 
Mequanint, K., Sheardown, H., 2-Methacryloyloxyethyl N-butylcarbamate: a new co-monomer for synthesis of polyurethane hydrogels with improved mechanical properties for biomedical applications (2005) Journal of Biomaterials Science Polymer Edition, 16 (10), pp. 1303-1318; 
Horbett, T.A., Adsorption of proteins from plasma to a series of hydrophilic-hydrophobic copolymers. II. Compositional analysis with the prelabeled protein technique (1981) Journal of Biomedical Materials Research, 15 (5), pp. 673-695; 
Feng, L., Andrade, J.D., Protein adsorption on low-temperature isotropic carbon. 3. isotherms, competitivity, desorption and exchange of human albumin and fibrinogen (1994) Biomaterials, 15 (5), pp. 323-333; 
Pitt, W.G., Cooper, S.L., Albumin adsorption on alkyl chain derivatized polyurethanes. 1. The effect of C-18 alkylation (1988) Journal of Biomedical Materials Research, 22 (5), pp. 359-382; 
Markiewski, M.M., Nilsson, B., Ekdahl, K.N., Mollnes, T.E., Lambris, J.D., Complement and coagulation: strangers or partners in crime? (2007) Trends in Immunology, 28 (4), pp. 184-192; 
Zhang, Z., Zhang, M., Chen, S., Horbett, T.A., Ratner, B.D., Jiang, S., Blood compatibility of surfaces with superlow protein adsorption (2008) Biomaterials, 29 (32), pp. 4285-4291; 
Grunkemeier, J.M., Tsai, W.B., Horbett, T.A., Hemocompatibility of treated polystyrene substrates: contact activation, platelet adhesion, and procoagulant activity of adherent platelets (1998) Journal of Biomedical Materials Research, 41 (4), pp. 657-670; 
Gorbet, M.B., Sefton, M.V., Biomaterial-associated thrombosis: roles of coagulation factors, complement, platelets and leukocytes (2004) Biomaterials, 25 (26), pp. 5681-5703
},
	month = {2009///},
	pages = {5541 - 5551},
	abstract = {This work intended to create a nanostructured biomaterial that would bind albumin in a selective and reversible way in order to inhibit the adsorption of other blood proteins and therefore minimize activation of coagulation. Different levels of C18 ligand have been immobilized on poly(2-hydroxyethyl methacrylate) (pHEMA). We hypothesize that samples with intermediate amounts of C18 ligand would allow albumin to recognize them and bind through its hydrophobic pockets specific for long chain fatty acids. Surface characterization has confirmed increasing amounts of C18 ligand on pHEMA as the percentage of C18 in solution increases, with maximum coverage achieved in 10\% C18 samples. Adsorption from pure albumin solution revealed a small decrease in albumin adsorption from pHEMA to 1\% C18 and 2.5\% C18 samples, but on surfaces with 5\% or higher C18 the amount of adsorbed albumin increased as the percentage of C18 increased. Competitive adsorption studies in the presence of both albumin and fibrinogen, and in the presence of all plasma proteins showed that 1\% C18 and 2.5\% C18 were the only surfaces selective for albumin, and that the presence of all plasma proteins may even potentiate albumin adsorption. Reversibility studies demonstrated that both 2.5\% C18 and 5\% C18 samples exchange                        125I-albumin selectively in the presence of both unlabeled albumin and plasma, but 2.5\% C18 samples presented higher exchangeability rates (58\%). Clotting times using recalcified plasma revealed that samples with none or small amounts of C18 (pHEMA to 5\% C18) did not shorten the clotting time compared to the negative control (polystyrene), indicating low activation of the intrinsic coagulation cascade. {\textcopyright} 2009 Elsevier Ltd. All rights reserved.
},
	keywords = {Adsorption, article, Biocompatible Materials, Biomaterials, blood clotting time, Blood Coagulation Tests, Body fluids, Clotting time, Coagulation, Coated Materials, Biocompatible, concentration response, controlled study, Fatty acids, fibrinogen, human serum albumin, hydrogel, Hydrogels, hydrophilicity, Ligands, long chain fatty acid, materials testing, Plasmas, PolyHEMA, Polyhydroxyethyl Methacrylate, polymacon, Polymer blends, polystyrene, Polystyrenes, priority journal, Protein adsorption, protein binding, Proteins, Serum Albumin, Surface modification, surface property, Surface treatment},
	isbn = {01429612 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-68549112719\&partnerID=40\&md5=aa1dd37881210211ef398092a3be6174},
	author = {Gon{\c c}alves, I.C. and Martins, M.C.L. and Barbosa, M.A. and Ratner, B.D.}
}
@article {2309,
	title = {Selective protein adsorption modulates platelet adhesion and activation to oligo(ethylene glycol)-terminated self-assembled monolayers with C18 ligands},
	journal = {Journal of Biomedical Materials Research - Part AJ. Biomed. Mater. Res. Part A},
	volume = {89},
	year = {2009},
	note = {Cited By (since 1996): 11Export Date: 21 November 2012Source: ScopusCODEN: JBMRCdoi: 10.1002/jbm.a.32011PubMed ID: 18442116Language of Original Document: EnglishCorrespondence Address: Gon{\c c}alves, I. C.; INEB-Instituto de Engenharia Biom{\'e}dica, Laborat{\'o}rio de Biomateriais, Universidade do Porto, Run do Campo Alegre, 823, 4150-180 Porto, Portugal; email: icastro@ineb.up.ptChemicals/CAS: fibrinogen, 9001-32-5; glutaraldehyde, 111-30-8, 37245-61-7; human serum albumin, 9048-49-1; Carbon, 7440-44-0; Ethylene Glycol, 107-21-1; Ligands; Serum AlbuminReferences: Nath, N., Hyun, J., Ma, H., Chilkoti, A., Surface engineering strategies for control of protein and cell interactions (2004) Surf Sci, 570, pp. 98-110;Mao, C., Qiu, Y.Z., Sang, H.B., Mei, H., Zhu, A.P., Shen, J., Lin, S.C., Various approaches to modify biomaterial surfaces for improving hemocompatibility (2004) Adv Colloid Interface Sci, 110, pp. 5-17; 
Gorbet, M.B., Sefton, M.V., Biomaterial-associated thrombosis: Roles of coagulation factors, complement, platelets and leukocytes (2004) Biomaterials, 25, pp. 5681-5703; 
Kottkemarchant, K., Anderson, J.M., Umemura, Y., Marchant, R.E., Effect of albumin coating on the in vitro blood compatibility of dacron arterial prostheses (1989) Biomaterials, 10, pp. 147-155; 
Munro, M.S., Quattrone, A.J., Ellsworth, S.R., Kulkarni, P., Eberhart, R.C., Alkyl substituted polymers with enhanced albumin affinity (1981) Trans Am Soc Artif Intern Organs, 27, pp. 499-503; 
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Rodrigues, S.N., Goncalves, I.C., Martins, M.C.L., Barbosa, M.A., Ralner, B.D., Fibrinogen adsorption, platelet adhesion and activation on mixed hydroxyl-/methyl-terminated self-assembled monolayers (2006) Biomaterials, 27, pp. 5357-5367; 
Frank, R.D., Dresbach, H., Thelen, H., Sieberth, H.G., Glutardialde- hyde induced fluorescence technique (GIFT): A new method for the imaging of platelet adhesion on biomaterials (2000) J Biomed Mater Res, 52, pp. 374-381; 
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Barbosa, J.N., Barbosa, M.A., Aguas, A.P., Inflammatory responses and cell adhesion to self-assembled monolayers of alkanethio- lates on gold (2004) Biomaterials, 25, pp. 2557-2563
},
	month = {2009///},
	pages = {642 - 653},
	abstract = {This study focuses on the selective binding of albumin to a nanostructured surfaces to inhibit other blood proteins from adsorbing thereby reducing platelet adhesion and activation. Tetra (ethylene-glycol)-terminated self- assembled monolayers (EG4 SAMs) with different percentages of CI 8 ligands on the surface were characterized by contact angle measurements, X-ray photoelectron microscopy, infrared reflection-absorption spectroscopy, and ellipsometry. A specific surface (2.5\% C18 SAM) was found to be selective for human serum albumin (HSA) in the presence of both albumin and fibrinogen (HFG). The importance of this concentration of C18 ligands was stressed in reversibility studies since that surface exchanged almost all the preadsorbed HSA by HSA in solution, but not by HFG. The effect of protein adsorption in the subsequent adhesion and activation of platelets was studied by pre-immersing the surfaces in albumin and plasma before contact with platelets. Scanning electron microscopy and glutaraldehyde induced fluorescence technique images showed that as surfaces got more hydrophobic due to the immobilization of C18 ligands, the number of adherent platelets increased and their morphology changed from round to fully spread. Pre-immersion in HSA led to an 80{\textdegree}/o decrease in platelet adhesion and reduction of activation. Pre-immersion in 1\% plasma was only relevant in 2.5\% CI 8 SAMs since this was the only surface that demonstrated less adhesion of platelets comparing with buffer pre-immersion. However, they still adsorb more platelets then when HSA was preadsorbed. This was confirmed in competition studies between HSA and plasma that suggested that other plasma proteins were also adsorbing to this surface. {\textcopyright} 2008 Wiley Periodicals, Inc.},
	keywords = {Absorption spectroscopy, Acoustic microscopes, Adhesion, Adsorption, Albumin, Aldehydes, Angle measurement, article, Biological materials, Biomaterials, Blood Platelets, Blood protein, Blood substitutes, Carbon, Cell Shape, chemical composition, Concentration of, Contact angle, controlled study, Ethylene, Ethylene Glycol, ethylene glycol derivative, fibrinogen, Fluorescence technique, glutaraldehyde, gold nanoparticle, human, human serum albumin, Human serum albumins, Humans, hydrophobicity, Infrared reflection absorption spectroscopy, infrared spectroscopy, ligand, Ligands, Nanostructured surface, normal human, Oligo(ethylene glycol), Photoelectron spectroscopy, plasma, Plasma diagnostics, Plasma protein, Plasmas, Platelet adhesion, Platelet Adhesiveness, Platelets, Protein adsorption, protein binding, Proteins, Sams, Scanning electron microscopy, Selective binding, Selective protein adsorption, self assembled monolayer, Self assembled monolayers, Self-assembled monolayers, Serum Albumin, Specific surface, Spectrophotometry, Infrared, Surface Properties, surface property, thrombocyte activation, thrombocyte adhesion, thrombocyte shape, X ray photoelectron spectroscopy, X-ray photoelectron microscopy},
	isbn = {15493296 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-66249128976\&partnerID=40\&md5=0be21ad44fe5cf556598975ea1655bed},
	author = {Gon{\c c}alves, I.C. and Martins, M.C.L. and Barbosa, M.A. and Naeemi, E. and Ratner, B.D.}
}
@article {2406,
	title = {Adsorption of albumin on prosthetic materials: Implication for tribological behavior},
	journal = {Journal of Biomedical Materials Research - Part AJ. Biomed. Mater. Res. Part A},
	volume = {78},
	year = {2006},
	note = {Cited By (since 1996): 25Export Date: 21 November 2012Source: ScopusCODEN: JBMRCdoi: 10.1002/jbm.a.30754PubMed ID: 16739106Language of Original Document: EnglishCorrespondence Address: Serro, A.P.; Centro de Qu{\'\i}mica Estrutural, Instituto Superior T{\'e}cnico, Av. Rovisco Pais, 1049-001 Lisboa, Portugal; email: anapaula.serro@ist.utl.ptChemicals/CAS: aluminum oxide, 1302-74-5, 1318-23-6, 1344-28-1, 14762-49-3; iodine 125, 14158-31-7, 22822-81-7; molybdenum, 7439-98-7; protein, 67254-75-5; stainless steel, 12597-68-1; Albumins; Biocompatible MaterialsTradenames: CHIRULEN, Poly Hi Solidur, GermanyManufacturers: Maret, Switzerland; MediMet, Germany; Poly Hi Solidur, GermanyReferences: Widmer, M.R., Heuberger, M., V{\"o}r{\"o}s, J., Spencer, N.D., Influence of polymer surface chemistry on frictional properties under protein-lubrication conditions: Implications for hip-implant design (2001) Tribol Lett, 10, pp. 111-116;Saikko, V., Effect of lubricant protein concentration on the wear of ultrahigh molecular weight polyethylene sliding against a CoCr counterface (2003) Trans ASME, 125, pp. 638-642; 
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Gispert, M.P., Serro, A.P., Cola{\c c}o, R., Saramago, B., Friction and wear mechanisms in hip prosthesis: Comparison of joint materials behaviour in several lubricants (2006) Wear, 260, pp. 149-158; 
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},
	month = {2006///},
	pages = {581 - 589},
	abstract = {The orthopedic prosthesis used to substitute damaged natural joints are lubricated by a pseudosynovial fluid that contains biological macromolecules with potential boundary lubrication properties. Proteins are some of those macromolecules whose role in the lubrication process is not yet completely understood. In a previous work, we investigated the influence of the presence of albumin, the major synovial protein, upon the tribological behavior of three of the most used pairs of artificial joint materials: ultra high molecular weight polyethylene (UHMWPE) against counterfaces of alumina, CoCrMo alloy, and 316L stainless steel. Albumin was found to cause a significant decrease in the friction coefficient when the counterfaces were metallic because transfer of UHMWPE was avoided, but this effect was much weaker in the case of alumina. The objective of the present work was to look for an explanation for these differences in tribological behavior in terms of albumin adsorption. With this goal, studies on adsorption of bovine serum albumin (BSA) on the counterface materials, from a biological model fluid (Hanks{\textquoteright} balanced salt solution), were carried out using radiolabeled albumin (                        125I-BSA), X-ray photoelectron spectroscopy, and atomic force microscopy. The conclusion from all techniques is that the driving force for albumin adsorption is higher on the metals than on alumina. These results confirm that the greater the amount of protein adsorbed on the counterface, the more efficient is the protection against the transfer of polymeric film to the counterface. {\textcopyright} 2006 Wiley Periodicals, Inc.
},
	keywords = {Adsorption, Albumin, Albumin adsorption, Albumins, Alumina, aluminum oxide, article, Atomic force microscopy, balanced salt solution, Biocompatible Materials, Body fluids, bovine serum albumin, chromium derivative, Cobalt alloy, Cobalt alloys, cobalt derivative, force, Friction, iodine 125, isotope labeling, joint fracture, Joints (anatomy), lubrication, macromolecule, metal, molecular weight, molybdenum, orthopedic prosthesis, orthopedics, Polyethylenes, polymer, Prostheses and Implants, prosthesis material, Prosthetics, protein, Proteins, Pseudosynovial fluid, Stainless steel, Thermodynamics, Tribology, ultra high molecular weight polyethylene, Ultra high molecular weight polyethylene (UHMWPE), X ray photoelectron spectroscopy},
	isbn = {00219304 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-33747426950\&partnerID=40\&md5=1728518c691365be3d5b3733dec3d60f},
	author = {Serro, A.P. and Gispert, M.P. and Martins, M.C.L. and Brogueira, P. and Cola{\c c}o, R. and Saramago, B.}
}
@book {2414,
	title = {Calcium phosphate microspheres for localised delivery of a therapeutic enzyme},
	series = {Key Engineering MaterialsKey Eng Mat},
	volume = {309-311 II},
	year = {2006},
	note = {Export Date: 21 November 2012Source: ScopusCODEN: KEMAELanguage of Original Document: EnglishCorrespondence Address: Barrias, C.C.; INEB - Instituto de Engenharia Biom{\'e}dica, Laborat{\'o}rio de Biomateriais, R. Campo Alegre 823, 4150-180 Porto, Portugal; email: ccbarrias@ineb.up.ptReferences: Barrias, C.C., Ribeiro, C.C., Barbosa, M.A., (2004) Key Eng. Mater., 254-256, p. 877;Barrias, C.C., Ribeiro, C.C., Lamghari, M., Miranda, C.S., Barbosa, M.A., (2005) J. Biomed. Mater. Res. A, 72 A, p. 57; 
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Barrias, C.C., Martins, M.A., Miranda, M.A., Barbosa, M.A., (2005) Biomaterials, 26, p. 2695
},
	month = {2006///},
	pages = {903 - 906},
	abstract = {The ability of calcium titanium phosphate (CTP) and hydroxyapatite (HAp) microspheres to reversibly adsorb the enzyme glucocerebrosidase (GCR) while preserving its biological activity, and efficiently deliver it to Gaucher disease (GD) fibroblasts was investigated. CTP microspheres adsorbed ca. 3.6-fold more GCR than HAp microspheres. The activity of adsorbed GCR was higher than the free enzyme in the case of CTP microspheres and lower when HAp was used. GCR release from both types of microspheres was characterized by the initial elution of a large percentage of enzyme followed by a delayed release that extended for at least 30 days. Released GCR was internalized by GD fibroblasts increasing their intracellular enzymatic activity. In cells treated with the same amount of GCR-loaded CTP microspheres or free-GCR a higher intracellular activity was detected in the former case, suggesting an improved efficacy.},
	keywords = {Adsorption, Biocompatibility, biological activity, Biomaterials, Calcium Compounds, Calcium titanium phosphate, Calcium titanium phosphate (CTP), Cells, Enzyme adsorption, Enzymes, hydroxyapatite, Microspheres},
	isbn = {10139826 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-33645396489\&partnerID=40\&md5=de3cf8530e8c690b254fed782b964340},
	author = {Barrias, C.C. and Ribeiro, C.C. and Martins, M.C.L. and Barbosa, M.A. and Rodrigues, D. and Miranda, M.C.S.}
}
@article {2392,
	title = {Fibrinogen adsorption, platelet adhesion and activation on mixed hydroxyl-/methyl-terminated self-assembled monolayers},
	journal = {BiomaterialsBiomaterials},
	volume = {27},
	year = {2006},
	note = {Cited By (since 1996): 70Export Date: 21 November 2012Source: ScopusCODEN: BIMADdoi: 10.1016/j.biomaterials.2006.06.010PubMed ID: 16842847Language of Original Document: EnglishCorrespondence Address: Martins, M.C.L.; INEB - Instituto de Engenharia Biom{\'e}dica, Laborat{\'o}rio de Biomateriais, Universidade do Porto, Rua do Campo Alegre, 823, 4150-180 Porto, Portugal; email: cmartins@ibmc.up.ptChemicals/CAS: fibrinogen, 9001-32-5; glutaraldehyde, 111-30-8, 37245-61-7; gold, 7440-57-5; thiol derivative, 13940-21-1; Alkanes; Biocompatible Materials; Fibrinogen, 9001-32-5; hydroxide ion, 14280-30-9; Hydroxides; Sulfhydryl CompoundsReferences: Savage, B., Ruggeri, Z.M., Selective recognition of adhesive sites in surface-bound fibrinogen by glycoprotein-iib-iiia on nonactivated platelets (1991) J Biol Chem, 266 (17), pp. 11227-11233;Tsai, W.B., Grunkemeier, J.M., McFarland, C.D., Horbett, T.A., Platelet adhesion to polystyrene-based surfaces preadsorbed with plasmas selectively depleted in fibrinogen, fibronectin, vitronectin, or von Willebrand{\textquoteright}s factor (2002) J Biomed Mater Res, 60 (3), pp. 348-359; 
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Gon{\c c}alves, I.C., Martins, M.C.L., Barbosa, M.A., Ratner, B.D., Protein adsorption on 18-alkyl chains immobilized on hydroxyl-terminated self-assembled monolayers (2005) Biomaterials, 26 (18), pp. 3891-3899; 
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Frank, R.D., Dresbach, H., Thelen, H., Sieberth, H.G., Glutaraldehyde induced fluorescence technique (GIFT): a new method for the imaging of platelet adhesion on biomaterials (2000) J Biomed Mater Res, 52 (2), pp. 374-381; 
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},
	month = {2006///},
	pages = {5357 - 5367},
	abstract = {The effect of surface wettability on fibrinogen adsorption, platelet adhesion and platelet activation was investigated using self-assembled monolayers (SAMs) containing different ratios of longer chain methyl- and shorter chain hydroxyl-terminated alkanethiols (C15CH3 vs. C11OH) on gold. Protein adsorption studies were performed using radiolabeled human fibrinogen (HFG). Platelet adhesion and activation studies with and without pre-adsorbed fibrinogen, albumin and plasma were assessed using scanning electron microscopy (SEM) and a glutaraldehyde-induced fluorescence technique (GIFT). Results demonstrated a linear decrease of HFG adsorption with the increase of OH groups on the monolayer (increase of the hydrophilicity). Platelet adhesion and activation also decrease with increase of hydrophilicity of surface. Concerning SAMs pre-immersed in proteins, fibrinogen adsorption was related with high platelet adhesion and activation. The passivant effect of albumin on platelet adhesion and activation was only demonstrated on SAMs contained C11OH. When all the blood proteins are present (plasma) platelet adhesion was almost absent on SAMs with 65\% and 100\% C11OH. This could be explained by the higher albumin affinity of the SAMs with 65\% C11OH and the lower total protein adsorption associated with SAMs with 100\% C11OH. {\textcopyright} 2006 Elsevier Ltd. All rights reserved.},
	keywords = {Adsorption, Albumin, alkane derivative, Alkanes, article, binding affinity, Biocompatible Materials, Blood Platelets, Cells, Cultured, Chemical reactions, controlled study, Crystallization, fibrinogen, Fluorescence, fluorescence analysis, glutaraldehyde, gold, human, human cell, Humans, hydrophilicity, Hydroxides, hydroxyl group, materials testing, methyl group, Methylation, monolayer culture, Monolayers, normal human, Organic compounds, plasma, Plasma protein, Platelet activation, Platelet adhesion, Platelet Adhesiveness, priority journal, Protein adsorption, protein binding, Proteins, Radiolabeled human fibrinogen (HFG), Scanning electron microscopy, Self assembled, SEM, Sulfhydryl Compounds, surface property, thiol derivative, thrombocyte adhesion, wettability},
	isbn = {01429612 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-33746216936\&partnerID=40\&md5=c2c54ad0448df431fbd884394915eb51},
	author = {Rodrigues, S.N. and Gon{\c c}alves, I.C. and Martins, M.C.L. and Barbosa, M.A. and Ratner, B.D.}
}
@article {2441,
	title = {Improving the adhesion of poly(ethylene terephthalate) fibers to poly(hydroxyethyl methacrylate) hydrogels by ozone treatment: Surface characterization and pull-out tests},
	journal = {PolymerPolymer},
	volume = {46},
	year = {2005},
	note = {Cited By (since 1996): 6Export Date: 21 November 2012Source: ScopusCODEN: POLMAdoi: 10.1016/j.polymer.2005.08.033Language of Original Document: EnglishCorrespondence Address: Ferreira, L.; Instituto de Engenharia Biom{\'e}dica, Laborat{\'o}rio de Biomateriais, Rua do Campo Alegre, 823, 4150-180 Porto, Portugal; email: lino@mit.eduReferences: Hart, B.L., Deyo, R.A., Cherkin, D.C., (1995) Spine, 20, pp. 11-19;Bao, Q.-B., McCullen, G.M., Higham, P.A., Dumbleton, J.H., Yuan, H.A., (1996) Biomaterials, 17, pp. 1157-1167; 
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},
	month = {2005///},
	pages = {9840 - 9850},
	abstract = {This work reports a methodology to improve the adhesion between poly(ethylene terephthalate) (PET) fibers and poly(hydroxyethyl methacrylate) (pHEMA) hydrogels by treating PET with ozone. The surface chemistry of PET was examined by water contact angle measurements, X-ray photoelectron spectroscopy (XPS), infrared reflection absorption spectroscopy (IRAS) and attenuated total reflectance infrared spectroscopy (ATR-IR) yielding information about the chemical functionalities at depths upon 0.6 μm. Ozone treatment introduces several polar groups in the surface of PET through oxidation and chain scission resulting in increased wettability. These groups include mostly carboxylic and anhydride groups and in small extent hydroxyl groups. Atomic force microscopy (AFM) analysis shows that the surface of ozone-treated PET films is fully covered with spherical particles that are removed after washing the film with water. During the washing step carboxylic functionalities were removed preferentially, as demonstrated by XPS and IR analysis. According to pull-out tests, PET monofilaments and bundles treated by ozone had a higher adhesion to pHEMA hydrogels than untreated ones. The apparent interfacial shear strength is 65\% higher on pHEMA hydrogel containing an ozonated than an untreated PET monofilament. In addition, the force to pull-out an ozone-treated PET bundle from pHEMA hydrogel is ca. 81\% higher than the one observed for the untreated bundle. {\textcopyright} 2005 Elsevier Ltd. All rights reserved.},
	keywords = {Adhesion, Atomic force microscopy, Contact angle, hydrogel, Hydrogels, infrared spectroscopy, Oxidation, Ozone, ozone treatment, Ozone treatments, Poly(ethylene terephthalate), polyethylene terephthalate fiber, Polyethylene terephthalates, Polymethyl methacrylates, pull-out, Pull-out tests, Surface characterization, Surface chemistry, surface property, X ray photoelectron spectroscopy},
	isbn = {00323861 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-26844540116\&partnerID=40\&md5=bebe6186e9e73c41648eedee7d5c0f61},
	author = {Ferreira, L. and Evangelista, M.B. and Martins, M.C.L. and Granja, P.L. and Esteves, J.L. and Barbosa, M.A.}
}
@article {2512,
	title = {Albumin adsorption on alkanethiols self-assembled monolayers on gold electrodes studied by chronopotentiometry},
	journal = {BiomaterialsBiomaterials},
	volume = {24},
	year = {2003},
	note = {Cited By (since 1996): 31Export Date: 21 November 2012Source: ScopusCODEN: BIMADdoi: 10.1016/S0142-9612(03)00244-8PubMed ID: 12818541Language of Original Document: EnglishCorrespondence Address: Martins, M.C.L.; INEB - Inst. de Engenharia Biomed., Laborat{\'o}rio de Biomateriais, Rua do Campo Alegre, 823, 4150-180 Porto, Portugal; email: cmartins@ibmc.up.ptChemicals/CAS: gold, 7440-57-5; thiol derivative, 13940-21-1; water, 7732-18-5; Albumins; Alkanes; Biocompatible Materials; Gold, 7440-57-5; Serum Albumin; Sulfhydryl CompoundsReferences: Ratner, B.D., Hoffman, A.S., Schoen, F.J., Lemons, J.L., (1996) Biomaterials science - an introduction to materials in medicine, , San Diego, CA, USA: Academic Press;Nakanishi, K., Sakiyama, T., Imamura, K., On the adsorption of proteins on solid surfaces, a common but very complicated phenomenon (2001) J Biosci Bioeng, 91, pp. 233-244; 
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},
	month = {2003///},
	pages = {3697 - 3706},
	abstract = {Chronopotentiometry was used to study the adsorption of human serum albumin (HSA) to self-assembled monolayers with the following terminal functional groups: CH                        3, COOH and OH. Surfaces were characterized by X-ray photoelectron spectroscopy, water contact angle measurements and cyclic voltammetry. HSA coverage of the different SAMs was investigated by chronopotentiometry and the total amount of adsorbed protein was determined using radiolabelled albumin. Both techniques have demonstrated that HSA adsorption to the different SAM-modified electrodes increases in the following order: OH\&lt;COOH\&lt;CH
                        3-terminated SAMs. A good correlation between coverage and total amount of HSA adsorbed was observed for long adsorption times (900s). {\textcopyright} 2003 Elsevier Science Ltd. All rights reserved.
},
	keywords = {Adsorption, Albumin, Albumin adsorption, Albumins, alkane, Alkanes, article, Biocompatible Materials, biomaterial, Biomaterials, carboxyl group, Chemical modification, Chronopotentiometry, Contact angle, correlation analysis, cyclic potentiometry, Cyclic voltammetry, electrochemistry, electrode, Electron Probe Microanalysis, Functional groups, gold, Humans, hydroxyl group, isotope labeling, methyl group, Monolayers, potentiometry, priority journal, protein analysis, Self assembly, Self-assembled monolayers, Serum Albumin, Sulfhydryl Compounds, Surface modification, Surface Properties, surface property, temperature, thiol derivative, Time Factors, Water, X ray photoelectron spectroscopy},
	isbn = {01429612 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0038802804\&partnerID=40\&md5=d9b75bc199d3c909e08c53f4de329ce5},
	author = {Martins, M.C.L. and Fonseca, C. and Barbosa, M.A. and Ratner, B.D.}
}
@article {2515,
	title = {Albumin and fibrinogen adsorption on Cibacron blue F3G-A immobilised onto PU-PHEMA (polyurethane-poly (hydroxyethylmethacrylate)) surfaces},
	journal = {Journal of Biomaterials Science, Polymer EditionJ. Biomater. Sci. Polym. Ed.},
	volume = {14},
	year = {2003},
	note = {Cited By (since 1996): 16Export Date: 21 November 2012Source: ScopusCODEN: JBSEEdoi: 10.1163/156856203766652057PubMed ID: 12807146Language of Original Document: EnglishCorrespondence Address: Martins, M.C.L.; Inst. de Engenharia Biomedica, Laborat{\'o}rio de Biomateriais, Rua do Campo Alegre 823, 4150-180 Porto, Portugal; email: cmartins@ibmc.up.ptChemicals/CAS: cibacron blue f3ga, 12236-82-7, 53127-08-5; dextran, 87915-38-6, 9014-78-2; fibrinogen, 9001-32-5; polymacon, 25053-81-0, 25249-16-5, 98932-78-6; polyurethan, 61789-63-7; Albumins; Biocompatible Materials; Cibacron Blue F 3GA, 12236-82-7; Fibrinogen, 9001-32-5; Membranes, Artificial; Polyhydroxyethyl Methacrylate, 25249-16-5; TriazinesReferences: Ratner, B.D., Hoffman, A.S., Schoen, F.J., Lemons, J.L., (1996) Biomaterials Science - an Introduction to Materials in Medicine, , (Eds), Academic Press, San Diego, CA;Greco, R.S., (1994) Implantation Biology, the Host Response and Biomedical Devices, , (Ed.), CRC Press, Ann Arbour, MI; 
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},
	month = {2003///},
	pages = {439 - 455},
	abstract = {In the present work, it is intended to study the effect of Cibacron blue F3G-A (CB) immobilised onto PU-PHEMA (polyurethane-poly(hydroxyethylmethacrylate)) surfaces on protein adsorption and bacterial adhesion. CB immobilisation was carried out by covalent binding between its triazine ring and the hydroxyl groups of the polymer. Characterisation of the films was carried out by attenuated total reflection Fourier transform infrared spectroscopy (ATR-FT-IR), contact angle measurements, X-ray photoelectron spectroscopy (XPS) and scanning electron microscopy (SEM). CB efficiency was evaluated using radiolabelled albumin and fibrinogen from pure solutions, mixtures of both and plasma. Bacterial adhesion tests before and after albumin pre-coating were also performed. The presence of CB increases albumin and fibrinogen adsorption to PU-PHEMA surfaces. The incorporation of CB onto the PU-PHEMA surface also increases bacterial adhesion. Although albumin pre-coating decreases bacterial adhesion onto PU (67\% decrease) and PU-PHEMA-CB (80\%), bacterial adhesion is always lower on PU and PU-PHEMA surfaces than on PU-PHEMA-CB. These results demonstrate that, in contrast to what has been described for CB bound to dextran, CB immobilisation on PU-PHEMA surfaces presents low selectivity to albumin and increased bacterial adhesion relatively to PU and PU-PHEMA surfaces.},
	keywords = {Adsorption, Albumin, Albumins, article, Bacterial adhesion, bacterium adherence, Biocompatible Materials, Chemical structure, Cibacron blue, cibacron blue f3ga, Contact angle, controlled study, covalent bond, dextran, fibrinogen, hydroxyl group, immobilization, infrared spectroscopy, isotope labeling, Membranes, Artificial, Microscopy, Electron, Scanning, nonhuman, PHEMA, Polyhydroxyethyl Methacrylate, polymacon, polyurethan, priority journal, Protein adsorption, Scanning electron microscopy, Spectroscopy, Fourier Transform Infrared, Staphylococcus epidermidis, Surface Properties, triazine derivative, Triazines, X ray photoelectron spectroscopy, XPS},
	isbn = {09205063 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0038316702\&partnerID=40\&md5=6f911799b67ba3289c643eb874879e1f},
	author = {Martins, M.C.L. and Wang, D. and Ji, J. and Feng, L. and Barbosa, M.A.}
}
@article {2517,
	title = {Albumin and fibrinogen adsorption on PU-PHEMA surfaces},
	journal = {BiomaterialsBiomaterials},
	volume = {24},
	year = {2003},
	note = {Cited By (since 1996): 41Export Date: 21 November 2012Source: ScopusCODEN: BIMADdoi: 10.1016/S0142-9612(03)00002-4PubMed ID: 12628827Language of Original Document: EnglishCorrespondence Address: Martins, M.C.L.; Laborat{\'o}rio de Biomateriais, Inst. de Engenharia Biom{\'e}dica, Rua do Campo Algre 823, Porto 4150-180, Portugal; email: cmartins@ibmc.up.ptChemicals/CAS: acrylic acid ethyl ester, 140-88-5; fibrinogen, 9001-32-5; poly(2 hydroxyethyl acrylate), 26022-14-0; polyetherurethan, 76600-67-4; polymacon, 25053-81-0, 25249-16-5, 98932-78-6; protein, 67254-75-5; Albumins; Biocompatible Materials; Fibrinogen, 9001-32-5; poly(2-hydroxyethyl acrylate), 26022-14-0; Polyhydroxyethyl Methacrylate, 25249-16-5; Water, 7732-18-5References: Ratner, B.D., Hoffman, A.S., Schoen, F.J., Lemons, J.L., (1996) Biomaterials science - An introduction to materials in medicine, , CA, USA, San Diego: Academic Press;Greco, R.S., (1994) Implantation biology, the host response and biomedical devices, , Ann Arbour, USA: CRC Press; 
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},
	month = {2003///},
	pages = {2067 - 2076},
	abstract = {Materials that adsorb specific proteins may find a variety of applications in the biomedical field. The aim of this study was the preparation of a hydrophilic surface, with low protein adsorption, to be used in the future as a support for the immobilisation of several species, e.g. Cibacron Blue F3G-A, which has been described to induce specific albumin adsorption. Poly(hydroxyethylmethacrylate) (PHEMA) and poly(hydroxyethylacrylate) (PHEA) were chosen as the hydrophilic surface because they can be easily polymerised and possess hydroxyl groups that can be used for the immobilisation of different compounds. Thin films of PHEMA and PHEA were successfully graft polymerised onto the surface of a commercial poly(etherurethane) (PU) using ceric ion as initiator. Grafting polymerisations were followed by mass gain and attenuated total reflection Fourier transform infrared spectroscopy (ATR-FTIR). Since stability tests demonstrated that only PU-PHEMA was stable in alkaline solutions, a necessary condition to future immobilisations, the investigation was focused on the coating of PU with PHEMA. PU-PHEMA films were characterised in detail using several techniques as mass gain, ATR-FTIR, contact angle measurements, X-ray photoelectron spectroscopy (XPS) and scanning electron microscopy (SEM). Protein adsorption was evaluated using radiolabelled albumin and fibrinogen from pure solutions and from mixtures of both proteins. PU surfaces modified with PHEMA have demonstrated low protein adsorption, showing their potential use as substrates. This opens the possibly of exploring the advantages of selective adsorption by appropriate immobilisation of specific molecules. {\textcopyright} 2003 Elsevier Science Ltd. All rights reserved.},
	keywords = {acrylic acid ethyl ester, Adsorption, Albumin, Albumins, article, ATR-FTIR, Biocompatible Materials, Chemical modification, Dose-Response Relationship, Drug, fibrinogen, film, Fourier transform infrared spectroscopy, Graft polymerisation, Humans, Hydrogen-Ion Concentration, Hydrophilic surfaces, hydrophilicity, hydroxyl group, infrared spectroscopy, isotope labeling, Microscopy, Electron, Scanning, molecular stability, Pellethane, PHEMA, poly(2 hydroxyethyl acrylate), polyetherurethan, Polyhydroxyethyl Methacrylate, polymacon, Polymerization, priority journal, protein, Protein adsorption, Proteins, Scanning electron microscopy, Spectrometry, X-Ray Emission, Spectroscopy, Fourier Transform Infrared, surface property, Thin films, unclassified drug, Water, X ray photoelectron spectroscopy},
	isbn = {01429612 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0037400503\&partnerID=40\&md5=dc989d7fe65e35d20f250cf3e7c245f9},
	author = {Martins, M.C.L. and Wang, D. and Ji, J. and Feng, L. and Barbosa, M.A.}
}
@article {2510,
	title = {Protein adsorption on mixtures of hydroxyl- and methyl-terminated alkanethiols self-assembled monolayers},
	journal = {Journal of Biomedical Materials Research - Part AJ. Biomed. Mater. Res. Part A},
	volume = {67},
	year = {2003},
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},
	month = {2003///},
	pages = {158 - 171},
	abstract = {The effect of surface composition and wettability on the adsorption of human serum albumin (HSA) was studied. Self-assembled monolayers (SAMs) containing mixtures of longer chain methyl- and shorter chain hydroxyl-terminated alkanethiols on gold were used to produce a range of surfaces with different wettabilities and exposed functional groups. Different SAMs were characterized by X-ray photoelectron spectroscopy, water contact angles, and Fourier transform infrared reflection absorption spectroscopy (IRAS). HSA adsorption onto the different SAMs was evaluated by contact angle measurements (wetting tension determinations), radiolabeling of proteins, and IRAS. Concerning HSA adsorption, all the techniques demonstrated higher HSA adsorption on more hydrophobic surfaces. The wetting tension measurements and IRAS suggested a gradual decrease of the HSA adsorption with increases of surface hydrophilicity. Radiolabeled albumin measurements also demonstrated a significant decrease of HSA adsorption on the pure hydroxyl-terminated SAMs. However, no significant differences were detected between mixed and pure methyl-terminated SAMs. Studies of HSA exchangeability with human fibrinogen have suggested that an ideal percentage of hydroxyl groups on the surface may increase albumin affinity without fibrinogen adsorption. {\textcopyright} 2003 Wiley Periodicals, Inc.},
	keywords = {Absorption spectroscopy, Adsorption, article, Biocompatible Materials, Contact angle, Contact angles, fourier transform infrared reflection absorption spectroscopy, Fourier transform infrared spectroscopy, Functional groups, gold, human serum albumin, hydrophilicity, hydrophobicity, IRAS, isotope labeling, measurement, Mixtures, monolayer culture, Monolayers, Protein adsorption, Proteins, Self-assembled monolayers, Spectrum Analysis, Sulfhydryl Compounds, surface property, tension, thiol derivative, Time Factors, wettability, X ray photoelectron spectroscopy, XPS},
	isbn = {00219304 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0344306504\&partnerID=40\&md5=cc1823cda1406a9f9572da09315251f7},
	author = {Martins, M.C.L. and Ratner, B.D. and Barbosa, M.A.}
}
