



@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.}
}
@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 {2872,
	title = {Biocompatibility of poly(lactic acid) with incorporated graphene-based materials},
	journal = {Colloids and Surfaces B: Biointerfaces},
	volume = {104},
	year = {2013},
	note = {Cited By (since 1996):3Export Date: 12 December 2013Source: Scopus},
	month = {2013///},
	pages = {229 - 238},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84872444845\&partnerID=40\&md5=7d61d767da7f0776cca70616b06301a9},
	author = {Pinto, A.M. and Moreira, S. and Gon{\c c}alves, I.C. and Gama, F.M. and Mendes, A.M. and Magalh{\~a}es, F.D.}
}
@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 {2839,
	title = {Graphene-based materials biocompatibility: A review},
	journal = {Colloids and Surfaces B: Biointerfaces},
	volume = {111},
	year = {2013},
	note = {Export Date: 12 December 2013Source: Scopus},
	month = {2013///},
	pages = {188 - 202},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84879808520\&partnerID=40\&md5=ae9e0dbaf79ff79a5f60800ac798b26d},
	author = {Pinto, A.M. and Gon{\c c}alves, I.C. and Magalh{\~a}es, F.D.}
}
@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 {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 {2183,
	title = {The effect of octadecyl chain immobilization on the hemocompatibility of poly (2-hydroxyethyl methacrylate)},
	journal = {BiomaterialsBiomaterials},
	volume = {33},
	year = {2012},
	note = {Export Date: 21 November 2012Source: ScopusCODEN: BIMADdoi: 10.1016/j.biomaterials.2012.07.007Language of Original Document: EnglishCorrespondence Address: Sperling, C.; Max Bergmann Center of Biomaterials Dresden, Leibniz Institute of Polymer Research Dresden, Hohe Str. 6, 01069 Dresden, Germany; email: sperling@ipfdd.deChemicals/CAS: isocyanate, 71000-82-3, 75-13-8; polymacon, 25053-81-0, 25249-16-5, 98932-78-6References: Gorbet, M.B., Sefton, M.V., Biomaterial-associated thrombosis: roles of coagulation factors, complement, platelets and leukocytes (2004) Biomaterials, 25, pp. 5681-5703;Cao, L., Sukavaneshvar, S., Ratner, B.D., Horbett, T.A., Glow discharge plasma treatment of polyethylene tubing with tetraglyme results in ultralow fibrinogen adsorption and greatly reduced platelet adhesion (2006) J Biomed Mater Res A, 79, pp. 788-803; 
Tanaka, M., Motomura, T., Kawada, M., Anzai, T., Kasori, Y., Shiroya, T., Blood compatible aspects of poly(2-methoxyethylacrylate) (PMEA)-relationship between protein adsorption and platelet adhesion on PMEA surface (2000) Biomaterials, 21, pp. 1471-1481; 
Martins, 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, 67 A, pp. 158-171; 
Ratner, B.D., Hoffman, A.S., Schoen, F.J., Lemons, J.L., (1996) Biomaterials science - an introduction to materials in medicine, pp. 237-46. , Academic Press, San Diego, CA, USA; 
Ratner, B.D., The catastrophe revisited: blood compatibility in the 21st century (2007) Biomaterials, 28, pp. 5144-5147; 
Ji, J., Barbosa, M.A., Feng, L.X., Shen, J.C., A novel urethane containing copolymer as a surface modification additive for blood contact materials (2002) J Mater Sci Mater Med, 13, pp. 677-684; 
Fujisawa, N., Bertram, C.D., Woodard, J.C., Poole-Warren, L.A., Schindhelm, K., Fluid dynamics of a textured blood-contacting surface (2001) J Biomech Eng, 123, pp. 97-105; 
Keogh, J.R., Eaton, J.W., Albumin binding surfaces for biomaterials (1994) J Lab Clin Med, 124, pp. 537-545; 
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; 
Sweryda-Krawiec, B., Devaraj, H., Jacob, G., Hickman, J.J., A new interpretation of serum albumin surface passivation (2004) Langmuir, 20, pp. 2054-2056; 
Amiji, M., Park, K., Surface modification of polymeric biomaterials with poly(ethylene oxide), albumin, and heparin for reduced thrombogenicity (1993) J Biomater Sci Polym Ed, 4, pp. 217-234; 
Roach, P., Parker, T., Gadegaard, N., Alexander, M.R., Surface strategies for control of neuronal cell adhesion: a review (2010) Surf Sci Rep, 65, pp. 145-173; 
Weng, Y.J., Hou, R.X., Li, G.C., Wang, J., Huang, N., Liu, H.Q., Immobilization of bovine serum albumin on TiO 2 film via chemisorption of H 3PO 4 interface and effects on platelets adhesion (2008) Appl Surf Sci, 254, pp. 2712-2719; 
Kang, I.-K., Kwon, B.K., Lee, J.H., Lee, H.B., Immobilization of proteins on poly(methyl methacrylate) films (1993) Biomaterials, 14, pp. 787-792; 
Graham, D.E., Phillips, M.C., Proteins at liquid interfaces. Kinetics of adsorption and surface denaturation (1979) J Colloid Interface Sci, 70, pp. 403-414; 
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, pp. 5541-5551; 
Streller, U., Sperling, C., Hubner, J., Hanke, R., Werner, C., Design and evaluation of novel blood incubation systems for in vitro hemocompatibility assessment of planar solid surfaces (2003) J Biomed Mater Res B, 66, pp. 379-390; 
Sperling, C., Maitz, M.F., Talkenberger, S., Gouzy, M.F., Groth, T., Werner, C., In vitro blood reactivity to hydroxylated and non-hydroxylated polymer surfaces (2007) Biomaterials, 28, pp. 3617-3625; 
Goncalves, I.C., Martins, M.C., Barbosa, M.A., Ratner, B.D., Protein adsorption on 18-alkyl chains immobilized on hydroxyl-terminated self-assembled monolayers (2005) Biomaterials, 26, pp. 3891-3899; 
Goertzen, W.K., Kessler, M.R., Dynamic mechanical analysis of carbon/epoxy composites for structural pipeline repair (2007) Compos Part B Eng, 38, pp. 1-9; 
Ebnesajjad, S., Surface and material characterization techniques (2006) Surface treatment of materials for adhesion bonding, pp. 43-73. , William Andrew Publishing; 
Meakin, J.R., Hukins, D.W.L., Aspden, R.M., Imrie, C.T., Rheological properties of poly(2-hydroxyethyl methacrylate) (pHEMA) as a function of water content and deformation frequency (2003) J Mater Sci Mater Med, 14, pp. 783-787; 
Kemal, E., Adesanya, K.O., Deb, S., Phosphate based 2-hydroxyethyl methacrylate hydrogels for biomedical applications (2011) J Mater Chem, 21, pp. 2237-2245; 
(2002) Biological evaluation of medical devices - part 4: selection of tests for interaction with blood, , ISO 1993-4:2002; 
Kern, W.P.D.A., Cleaning solutions based on hydrogen peroxide for use in silicon semiconductor technology (1970) RCA Rev, 31, pp. 187-206; 
Cras, J.J., Rowe-Taitt, C.A., Nivens, D.A., Ligler, F.S., Comparison of chemical cleaning methods of glass in preparation for silanization (1999) Biosens Bioelectron, 14, pp. 683-688; 
Sperling, C., Fischer, M., Maitz, M.F., Werner, C., Blood coagulation on biomaterials requires the combination of distinct activation processes (2009) Biomaterials, 30, pp. 4447-4456; 
Park, J.G., Ye, Q., Topp, E.M., Lee, C.H., Kostoryz, E.L., Misra, A., Dynamic mechanical analysis and esterase degradation of dentin adhesives containing a branched methacrylate (2009) J Biomed Mater Res B, 91, pp. 61-70; 
Hu, W.J., Eaton, J.W., Ugarova, T.P., Tang, L., Molecular basis of biomaterial-mediated foreign body reactions (2001) Blood, 98, pp. 1231-1238; 
Franc, R.D., Dresbach, H., Thelen, H., Sieberth, H.-G., Glutardialdehyde induced fluorescence technique (GIFT): a new method for the imaging of platelet adhesion on biomaterials (2000) J Biomed Mater Res, 52, pp. 374-381; 
Rodrigues, S.N., Goncalves, I.C., Martins, M.C., 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; 
Downer, A., Morris, N., Feast, W.J., Stickler, D., Polymer surface properties and their effect on the adhesion of Proteus mirabilis (2003) Proc Inst Mech Eng H, 217, pp. 279-289; 
Crespin, M., Moreau, N., Masereel, B., Feron, O., Gallez, B., Vander Borght, T., Surface properties and cell adhesion onto allylamine-plasma and amine-plasma coated glass coverslips (2011) J Mater Sci Mater Med, 22, pp. 671-682; 
Maboudian, R., Howe, R.T., Critical review: adhesion in surface micromechanical structures (1997) J Vac Sci Technol B, 15, pp. 1-20; 
G{\"u}le{\c c}, H.A., SarIoglu, K., Mutlu, M., Modification of food contacting surfaces by plasma polymerisation technique. Part I: determination of hydrophilicity, hydrophobicity and surface free energy by contact angle method (2006) J Food Eng, 75, pp. 187-195; 
Cowling, M.J., Hodgkiess, T., Parr, A.C., Smith, M.J., Marrs, S.J., An alternative approach to antifouling based on analogues of natural processes (2000) Sci Total Environ, 258, pp. 129-137; 
Kwok, C.S., 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; 
Gobel, R.J., Janatova, J., Googe, J.M., Apple, D.J., Activation of complement in human serum by some synthetic polymers used for intraocular lenses (1987) Biomaterials, 8, pp. 285-288; 
Payne, M.S., Horbett, T.A., Complement activation by hydroxyethyl-methacrylate-ethylmethacrylate copolymers (1987) J Biomed Mater Res, 21, pp. 843-859; 
Vasilev, K., Mierczynska, A., Hook, A.L., Chan, J., Voelcker, N.H., Short, R.D., Creating gradients of two proteins by differential passive adsorption onto a PEG-density gradient Biomaterials:392-7Ikeda, K., Nagasawa, K., Horiuchi, T., Tsuru, T., Nishizaka, H., Niho, Y., C5a induces tissue factor activity on endothelial cells (1997) Thromb Haemost, 77, pp. 394-398; 
Tedesco, F., Pausa, M., Nardon, E., Introna, M., Mantovani, A., Dobrina, A., The cytolytically inactive terminal complement complex activates endothelial cells to express adhesion molecules and tissue factor procoagulant activity (1997) J Exp Med, 185, pp. 1619-1627; 
Fischer, M., Sperling, C., Tengvall, P., Werner, C., The ability of surface characteristics of materials to trigger leukocyte tissue factor expression (2009) Biomaterials, 31, pp. 2498-2507; 
Iuliano, L., Colavita, A.R., Leo, R., Pratic{\`o}, D., Violi, F., Oxygen free radicals and platelet activation (1997) Free Radic Biol Med, 22, pp. 999-1006; 
Khodr, B., Khalil, Z., Modulation of inflammation by reactive oxygen species: implications for aging and tissue repair (2001) Free Radic Biol Med, 30, pp. 1-8; 
Mao, X-Y., Cheng, X., Wang, X., Wu, S-J., Free-radical-scavenging and anti-inflammatory effect of yak milk casein before and after enzymatic hydrolysis Food Chem;126:484-90Pawlak, K., Naumnik, B., Brzosko, S., Pawlak, D., Myliwiec, M., Oxidative stress - a link between endothelial injury, coagulation activation, and atherosclerosis in haemodialysis patients (2004) Am J Nephrol, 24, pp. 154-161; 
Nilsson, B., Ekdahl, K.N., Mollnes, T.E., Lambris, J.D., The role of complement in biomaterial-induced inflammation (2007) Mol Immunol, 44, pp. 82-94; 
Laudes, I.J., Chu, J.C., Sikranth, S., Huber-Lang, M., Guo, R.-F., Riedemann, N., Anti-C5a ameliorates coagulation/fibrinolytic protein changes in a rat model of sepsis (2002) Am J Pathol, 160, pp. 1867-1875
},
	month = {2012///},
	pages = {7677 - 7685},
	abstract = {Albumin-scavenging surfaces decorated with n-alkyl chains represent an established strategy for blood-contacting applications. To evaluate this concept, a set of poly (2-hydroxyethyl methacrylate) (pHEMA) films modified with different amounts of octadecyl isocyanate (C18) was investigated in an in vitro hemocompatibility assay using freshly drawn human whole blood. In addition, the hydrogel materials were thoroughly characterized with respect to changes in wettability and elasticity, which accompanied the gradual chemical modification of pHEMA. An increase of the surface C18 content induced enhanced hydrophobicity and stiffness. Immobilization of C18 chains was found to substantially reduce the coagulation activation and the complement activation by the pHEMA films. Platelet adhesion and degranulation (PF4 release) were similar on the modified and the unmodified pHEMA. Platelet adhesion to pHEMA hydrogels was lower than the polytetrafluoroethylene reference. We conclude that the immobilization of octadecyl chains improved the hemocompatibility of pHEMA materials under conditions that might be encountered in low shear blood flow. {\textcopyright} 2012 Elsevier Ltd.},
	keywords = {Adhesion, Albumin, article, Biological materials, Biomaterials, Blood, Blood flow, Chemical modification, Coagulation, controlled study, Degranulation, Elasticity, Haemocompatibility, Hemocompatibility, human, hydrogel, in vitro study, In-vitro, isocyanate, Octadecyl, octadecyl isocyanate, PHEMA, Platelet adhesion, Platelets, Poly(2-hydroxyethyl methacrylate), PolyHEMA, polymacon, priority journal, Protein adsorption, thrombocyte adhesion, unclassified drug, wettability, Whole blood},
	isbn = {01429612 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84865188580\&partnerID=40\&md5=81a8750115106c3d6e9fa2de862d9f70},
	author = {Fischer, M. and Baptista, C.P. and Gon{\c c}alves, I.C. and Ratner, B.D. and Sperling, C. and Werner, C. and Martins, C.L. 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; 
Wettero, J., Bengtsson, T., Tengvall, P., C1q-independent activation of neutrophils by immunoglobulin M-coated surfaces (2001) J Biomed Mater Res, 57, pp. 550-558; 
Yung, L.Y.L., Colman, R.W., Cooper, S.L., Neutrophil adhesion on polyurethanes preadsorbed with high molecular weight kininogen (1999) Blood, 94, pp. 2716-2724; 
Eriksson, C., Nygren, H., Polymorphonuclear leukocytes in coagulating whole blood recognize hydrophilic and hydrophobic titanium surfaces by different adhesion receptors and show different patterns of receptor expression (2001) J Lab Clin Med, 137, pp. 296-302; 
Tang, L.P., Eaton, J.W., Mechanism of acute inflammatory response to biomaterials (1994) Cell Mater, 4, pp. 429-436; 
Tang, L.P., Eaton, J.W., Inflammatory responses to biomaterials (1995) Am J Clin Pathol, 103, pp. 466-471; 
Jenney, C.R., Anderson, J.M., Adsorbed serum proteins responsible for surface dependent human macrophage behavior (1999) J Biomed Mater Res, 49, pp. 435-447; 
Collier, T.O., Anderson, J.M., Protein and surface effects on monocyte and macrophage adhesion, maturation, and survival (2002) J Biomed Mater Res, 60, pp. 487-496; 
Yun, J.K., Defife, K., Colton, E., Stack, S., Azeez, A., Cahalan, L., Verhoeven, M., Anderson, J.M., Human monocytemacrophage adhesion and cytokine production on surface-modified poly(tetrafluoroethylene hexafluoropropylene) polymers with and without protein preadsorption (1995) J Biomed Mater Res, 29, pp. 257-268; 
Ulman, A., Formation and structure of self-assembled monolayers (1996) Chem Rev, 96, pp. 1533-1554; 
Mrksich, M., Tailored substrates for studies of attached cell culture (1998) Cell Mol Life Sci, 54, pp. 653-662; 
Mrksich, M., Model substrates for studying and controlling cell adhesion (2000) Abstr Pap Am Chem Soc, 219, pp. U572-U572; 
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; 
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; 
Anderson, J.M., Biological responses to materials (2001) Annu Rev Mater Res, 31, pp. 81-110; 
Tang, L.P., Liu, L., Elwing, H.B., Complement activation and inflammation triggered by model biomaterial surfaces (1998) J Biomed Mater Res, 41, pp. 333-340; 
Bergman, A.J., Zygourakis, K., Migration of lymphocytes on fibronectin-coated surfaces: Temporal evolution of migratory parameters (1999) Biomaterials, 20, pp. 2235-2244; 
Taborelli, M., Eng, L., Descouts, P., Ranieri, J.P., Bellamkonda, R., Aebischer, P., Bovine serum-albumin conformation on methyl and amine functionalized surfaces compared by scanning force microscopy (1995) J Biomed Mater Res, 29, pp. 707-714; 
Liu, L., Elwing, H., Complement activation on thiol-modi.ed gold surfaces (1996) J Biomed Mater Res, 30, pp. 535-541; 
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; 
Hirata, I., Hioko, Y., Toda, M., Kitazawa, T., Murakami, Y., Kitano, E., Kitamura, H., Iwata, H., Deposition of complement protein C3b on mixed self-assembled monolayers carrying surface hydroxyl and methyl groups studied by surface plasmon resonance (2003) J Biomed Mater Res, 66 A, pp. 669-676. , Part A; 
Kalltorp, M., Oblogina, S., Jacobsson, S., Karlsson, A., Tengvall, P., Thomsen, P., In vivo cell recruitment, cytokine release and chemiluminescence response at gold, and thiol functionalized surfaces (1999) Biomaterials, 20, pp. 2123-2137; 
Brash, J.L., Tenhove, P., Protein adsorption studies on standard polymeric materials (1993) J Biomater Sci Polym Ed, 4, pp. 591-599; 
Brash, J.L., Tenhove, P., Effect of plasma dilution on adsorption of fibrinogen to solid-surfaces (1984) Thromb Haemost, 51, pp. 326-330; 
Tang, L.P., Ugarova, T.P., Plow, E.F., Eaton, J.W., Molecular determinants of acute inflammatory responses to biomaterials (1996) J Clin Invest, 97, pp. 1329-1334; 
Thomsen, P., Gretzer, C., Macrophage interactions with modified material surfaces (2001) Curr Opin Solid State Mater Sci, 5, pp. 163-176; 
Werthen, M., Sellborn, A., Kalltorp, M., Elwing, H., Thomsen, P., In vitro study of monocyte viability during the initial adhesion to albumin- and fibrinogen-coated surfaces (2001) Biomaterials, 22, pp. 827-832; 
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; 
Jenney, C.R., Anderson, J.M., Adsorbed IgG: A potent adhesive substrate for human macrophages (2000) J Biomed Mater Res, 50, pp. 281-290; 
Lindblad, M., Lestelius, M., Johansson, A., Tengvall, P., Thomsen, P., Cell and soft tissue interactions with methyl- and hydroxyl-terminated alkane thiols on gold surfaces (1997) Biomaterials, 18, pp. 1059-1068; 
Roach, P., Farrar, D., Perry, C.C., Interpretation of protein adsorption: Surface-induced conformational changes (2005) J Am Chem Soc, 127, pp. 8168-8173; 
Barbosa, J.N., Barbosa, M.A., Aguas, A.P., Adhesion of human leukocytes to biomaterials: An in vitro study using alkanethiolate monolayers with different chemically functionalized surfaces (2003) J Biomed Mater Res, 65 A, pp. 429-434. , Part A; 
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 {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; 
Eberhart, R.C., Munro, M.S., Williams, G.B., Kulkarni, P.V., Shannon, W.A., Brink, B.E., Fry, W.J., Albumin adsorption and retention on C-18-alkyl-derivatized polyurethane vascular grafts (1987) Artif Organs, 11, pp. 375-382; 
Frautschi, J.R., Munro, M.S., Lloyd, D.R., Eberhart, R.C., Alkyl derivatized cellulose-acetate membranes with enhanced albumin affinity (1983) Trans Am Soc Artif Intern Organs, 29, pp. 242-244; 
Pitt WG, Cooper SL. Albumin adsorption on alkyl chain derivatized polyurethanes. I. The effect of C-18 alkylation. T Biomed Mater Res 1988;22:359-382Johnston, E., Ratner, B.D., Protein Adsorption: Friend or Foe? (1998) Immobilized biomolecules in analysis: A practical approach, pp. 79-94. , Cass T, Ligler FS, editors, Oxford: Oxford University Press;; 
Ji, J., Feng, L.X., Barbosa, M.A., Stearyl poly(ethylene oxide) grafted surfaces for preferential adsorption of albumin (2001) Biomaterials, 22, pp. 3015-3023; 
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, pp. 945-954; 
Sigal, G.B., Mrksich, M., Whitesides, G.M., Effect of surface wettability on the adsorption of proteins and detergents (1998) J Am Chem Soc, 120, pp. 3464-3473; 
Palegrosdemange, C., Simon, E.S., Prime, K.L., Whitesides, G.M., Formation of self-assembled monolayers by chemisorption of derivatives of oligo(ethylene glycol) of structure Hs(Ch2)11 (Och2ch2)meta-Oh on gold (1991) J Am Chem Soc, 113, pp. 12-20; 
Goncalves, I.C., Martins, M.C.L., Barbosa, M.A., Ratner, B.D., Protein adsorption on 18-alkyl chains immobilized on hydroxyl-ter- minated self-assembled monolayers (2005) Biomaterials, 26, pp. 3891-3899; 
Martins MCL, Ratner BD, Barbosa MA. Protein adsorption on mixtures of hydroxyl- and methylterminated alkanethiols self-assembled monolavers. I Biomed Mater Res 2003;67A: 158-171Owens, D.K., Wendt, R.C., Estimation of surface free energy of polymers (1969) J Appl Polym Sci, 13, pp. 1741-1747; 
Sousa, S.R., Moradas Ferreira, P., Saramago, B., Viseu Melo, L., Barbosa, M.A., Human serum albumin adsorption on TiO 2 from single protein solutions and from plasma (2004) Langmuir, 20, pp. 9745-9754; 
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; 
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; 
Herrwerth, S., Eck, W., Reinhardt, S., Grunze, M., Factors that determine the protein resistance of oligoether self-assembled monolayers-internal hydrophilicity, terminal hydrophilicity, and lateral packing density (2003) J Am Chem Soc, 125, pp. 9359-9366; 
Harder, P., Grunze, M., Dahint, R., Whitesides, G.M., Laibinis, P.E., Molecular conformation in oligo(ethylene glycol)-terminated self-assembled monolayers on gold and silver surfaces deter-mines their ability to resist protein adsorption (1998) J Phys Chem B, 102, pp. 426-436; 
Schwendel, D., Dahint, R., Herrwerth, S., Schloerholz, M., Eck, W., Grunze, M., Temperature dependence of the protein resistance of poly- and oligo(ethylene glycol)-terminated alkanethiolate monolayers (2001) Langmuir, 17, pp. 5717-5720; 
Zhu, B., Eurell, T., Gunawan, R., Leckband, D., Chain-length dependence of the protein and cell resistance of oligo(ethylene glycol)-terminated self-assembled monolayers on gold (2001) J Biomed Mater Res, 56, pp. 406-416; 
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; 
Jenney, C.R., Anderson, J.M., Adsorbed serum proteins responsible for surface dependent human macrophage behavior (1999) J Biomed Mater Res, 49, pp. 435-447; 
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; 
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 {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; 
Kottkemarchant, K., Anderson, J.M., Umemura, Y., Marchant, R.E., Effect of albumin coating on the invitro blood compatibility of dacron arterial prostheses (1989) Biomaterials, 10 (3), pp. 147-155; 
Margel, S., Vogler, E.A., Firment, L., Watt, T., Haynie, S., Sogah, D.Y., Peptide, protein, and cellular interactions with self-assembled monolayer model surfaces (1993) J Biomed Mater Res, 27 (12), pp. 1463-1476; 
Tidwell, C.D., Ertel, S.I., Ratner, B.D., Tarasevich, B.J., Atre, S., Allara, D.L., Endothelial cell growth and protein adsorption on terminally functionalized, self-assembled monolayers of alkanethiolates on gold (1997) Langmuir, 13 (13), pp. 3404-3413; 
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; 
Peters, T., (1996) All about albumin: biochemistry, genetics and medical applications, , Academic Press Inc., San Diego, CA; 
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 A, 67 A (1), pp. 158-171; 
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; 
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; 
(1993) Iodine-125. A guide to radioiodination techniques, , Amersham Life Science, Little Chalfort; 
Porter, M.D., Bright, T.B., Allara, D.L., Chidsey, C.E.D., Spontaneously organized molecular assemblies. 4. Structural characterization of normal-alkyl thiol monolayers on gold by optical ellipsometry, infrared-spectroscopy, and electrochemistry (1987) J Am Chem Soc, 109 (12), pp. 3559-3568; 
Sigal, G.B., Mrksich, M., Whitesides, G.M., Effect of surface wettability on the adsorption of proteins and detergents (1998) J Am Chem Soc, 120 (14), pp. 3464-3473; 
Goodman, S.L., Sheep, pig, and human platelet-material interactions with model cardiovascular biomaterials (1999) J Biomed Mater Res, 45 (3), pp. 240-250; 
Slack, S.M., Horbett, T.A., Changes in fibrinogen adsorbed to segmented polyurethanes and hydroxyethylmethacrylate-ethylmethacrylate copolymers (1992) J Biomed Mater Res, 26 (12), pp. 1633-1649; 
Andrade, J.D., Hlady, V., Protein adsorption and materials biocompatibility-a tutorial review and suggested hypotheses (1986) Adv Polym Sci, 79, pp. 1-63; 
Roach, P., Farrar, D., Perry, C.C., Interpretation of protein adsorption: surface-induced conformational changes (2005) J Am Chem Soc, 127 (22), pp. 8168-8173; 
Silin, V., Weetall, H., Vanderah, D.J., SPR studies of the nonspecific adsorption kinetics of human IgG and BSA on gold surfaces modified by self-assembled monolayers (SAMs) (1997) J Colloid Interf Sci, 185 (1), pp. 94-103; 
Lin, Y., Wang, J., Wan, L.J., Fang, X.H., Study of fibrinogen adsorption on self-assembled monolayers on Au (1 1 1) by atomic force microscopy (2005) Ultramicroscopy, 105 (1-4), pp. 129-136; 
Norde, W., Favier, J.P., Structure of adsorbed and desorbed proteins (1992) Colloid Surf, 64 (1), pp. 87-93; 
Alfonsi-Hourdin, S., Longchamp, S., Gallet, O., Nigretto, J.M., Electrochemical processing of fibrinogen modified-graphite surfaces: effect on plasmin generation from adsorbed plasminogen (2006) Biomaterials, 27 (1), pp. 52-60; 
Tsai, W.B., Shi, Q., Grunkemeier, J.M., McFarland, C., Horbett, T.A., Platelet adhesion to radiofrequency glow-discharge-deposited fluorocarbon polymers preadsorbed with selectively depleted plasmas show the primary role of fibrinogen (2004) J Biomater Sci-Polym E, 15 (7), pp. 817-840; 
Stryer, L., (1998) Biochemistry. 4th ed., , WH Freeman, New York; 
Doolittle, R.F., Watt, K.W.K., Cottrell, B.A., Strong, D.D., Riley, M., Amino-acid sequence of the alpha-chain of human-fibrinogen (1979) Nature, 280 (5722), pp. 464-468; 
Kloczewiak, M., Timmons, S., Lukas, T.J., Hawiger, J., Platelet receptor recognition site on human-fibrinogen-synthesis and structure-function relationship of peptides corresponding to the carboxy-terminal segment of the gamma-chain (1984) Biochemistry, 23 (8), pp. 1767-1774; 
Tsai, W.B., Grunkemeier, J.M., Horbett, T.A., Variations in the ability of adsorbed fibrinogen to mediate platelet adhesion to polystyrene-based materials: a multivariate statistical analysis of antibody binding to the platelet binding sites of fibrinogen (2003) J Biomed Mater Res A, 67 A (4), pp. 1255-1268; 
Salsmann, A., Schaffner-Reckinger, E., Kabile, F., Plancon, S., Kieffer, N., A new functional role of the fibrinogen RGD motif as the molecular switch that selectively triggers integrin alpha IIb beta 3-dependent RhoA activation during cell spreading (2005) J Biol Chem, 280 (39), pp. 33610-33619; 
Lin, J.C., Chuang, W.H., Synthesis, surface characterization, and platelet reactivity evaluation for the self-assembled monolayer of alkanethiol with sulfonic acid functionality (2000) J Biomed Mater Res, 51 (3), pp. 413-423; 
Tanaka, M., Motomura, T., Kawada, M., Anzai, T., Kasori, Y., 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; 
Barbucci, R., Lamponi, S., Magnani, A., Fibrinogen conformation and platelet reactivity in relation to material-blood interaction: effect of stress hormones (2003) Biomacromolecules, 4 (6), pp. 1506-1513; 
Hylton, D.M., Shalaby, S.W., Latour, R.A., Direct correlation between adsorption-induced changes in protein structure and platelet adhesion (2005) J Biomed Mater Res A, 73 A (3), pp. 349-358; 
Brash, J.L., Tenhove, P., Protein adsorption studies on standard polymeric materials (1993) J Biomat Sci-Polym E, 4 (6), pp. 591-599
},
	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.}
}
