



@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.}
}
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},
	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},
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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 {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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},
	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; 
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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;; 
Li, L.Y., Chen, S.F., Zheng, J., Ratner, B.D., Jiang, S.Y., Protein adsorption on oligo(ethylene glycol)-terminated alkanethiolate self-assembled monolayers: The molecular basis for non-fouling behavior (2005) J Phys Chem B, 109, pp. 2934-2941; 
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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; 
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},
	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.}
}
