



@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; 
Keselowsky, B.G., Collard, D.M., Garc{\'\i}a, A.J., Surface chemistry modulates fibronectin conformation and directs integrin binding and specificity to control cell adhesion (2003) J Biomed Mater Res A, 66, pp. 247-259; 
Underwood, P.A., Bennett, F.A., A comparison of the biological activities of the cell-adhesive proteins vitronectin and fibronectin (1989) J Cell Sci, 93, pp. 641-649; 
Steele, J.G., Johnson, G., Underwood, P.A., Role of serum vitronectin and fibronectin in adhesion of fibroblasts following seeding onto tissue culture polystyrene (1992) J~Biomed Mater Res, 26, pp. 861-884; 
Steele, J.G., Dalton, B.A., Johnson, G., Underwood, P.A., Polystyrene chemistry affects vitronectin activity: an explanation for cell attachment to tissue culture polystyrene but not to unmodified polystyrene (1993) J Biomed Mater Res, 27, pp. 927-940; 
Underwood, P.A., Steele, J.G., Dalton, B.A., Effects of polystyrene surface chemistry on the biological activity of solid phase fibronectin and vitronectin, analysed with monoclonal antibodies (1993) J Cell Sci, 104, pp. 793-803; 
Suzuki, S., Oldberg, A., Hayman, E.G., Pierschbacher, M.D., Ruoslahti, E., Complete amino acid sequence of human vitronectin deduced from cDNA. Similarity of cell attachment sites in vitronectin and fibronectin (1985) EMBO J, 4, pp. 2519-2524; 
Lee, M.H., Ducheyne, P., Lynch, L., Boettiger, D., Composto, R.J., Effect of biomaterial surface properties on fibronectin-alpha5beta1 integrin interaction and cellular attachment (2006) Biomaterials, 27, pp. 1907-1916; 
Grinnell, F., Feld, M.K., Fibronectin adsorption on hydrophilic and hydrophobic surfaces detected by antibody binding and analyzed during cell adhesion in serum-containing medium (1982) J Biol Chem, 257, pp. 4888-4893; 
Sousa, S.R., Lamghari, M., Sampaio, P., Moradas-Ferreira, P., Barbosa, M.A., Osteoblast adhesion and morphology on TiO 2 depends on the competitive preadsorption of albumin and fibronectin (2008) J Biomed Mater Res A, 84, pp. 281-290; 
Fabrizius-Homan, D.J., Cooper, S.L., Competitive adsorption of vitronectin with albumin, fibrinogen, and fibronectin on polymeric biomaterials (1991) J Biomed Mater Res, 25, pp. 953-971; 
Bale, M.D., Wohlfahrt, L.A., Mosher, D.F., Tomasini, B., Sutton, R.C., Identification of vitronectin as a major plasma protein adsorbed on polymer surfaces of different copolymer composition (1989) Blood, 74, pp. 2698-2706; 
Thomas, C.H., McFarland, C.D., Jenkins, M.L., Rezania, A., Steele, J.G., Healy, K.E., The role of vitronectin in the attachment and spatial distribution of bone-derived cells on materials with patterned surface chemistry (1997) J Biomed Mater Res, 37, pp. 81-93; 
McFarland, C.D., Thomas, C.H., DeFilippis, C., Steele, J.G., Healy, K.E., Protein adsorption and cell attachment to patterned surfaces (2000) J Biomed Mater Res, 49, pp. 200-210; 
Love, J.C., 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; 
Mrksich, M., Whitesides, G.M., Using self-assembled monolayers to understand the interactions of man-made surfaces with proteins and cells (1996) Annu Rev Biophys Biomol Struct, 25, pp. 55-78; 
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; 
Faucheux, N., Schweiss, R., L{\"u}tzow, K., Werner, C., Groth, T., Self-assembled monolayers with different terminating groups as model substrates for cell adhesion studies (2004) Biomaterials, 25, pp. 2721-2730; 
Bernards, M.T., Jiang, S., pH-induced conformation changes of adsorbed vitronectin maximize its bovine aortic endothelial cell binding ability (2008) J Biomed Mater Res A; 
Martins, M.C., Ratner, B.D., Barbosa, M.A., Protein adsorption on mixtures of hydroxyl- and methyl-terminated alkanethiols self-assembled monolayers (2003) J~Biomed Mater Res A, 67, pp. 158-171; 
Rodrigues, S.N., Gon{\c c}alves, 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; 
Chamberlain, J., Yamagami, T., Colletti, E., Theise, N.D., Desai, J., Frias, A., Efficient generation of human hepatocytes by the intrahepatic delivery of clonal human mesenchymal stem cells in fetal sheep (2007) Hepatology, 46, pp. 1935-1945; 
(1993) Iodine-125. A guide to radioiodination techniques, , Amersham Life Science, Little Chalfort; 
Horbett, T.A., Techniques for protein adsorption studies (1986) Techniques of biocompatibility tests, pp. 183-214. , Williams D.F. (Ed), CRC Press Inc., Harcover; 
Arima, Y., Iwata, H., Effect of wettability and surface functional groups on protein adsorption and cell adhesion using well-defined mixed self-assembled monolayers (2007) Biomaterials, 28, pp. 3074-3082; 
Capadona, J.R., Collard, D.M., Garcia, A.J., Fibronectin adsorption and cell adhesion to mixed monolayers of tri(ethylene glycol)- and methyl-terminated alkanethiols (2003) Langmuir, 19, pp. 1847-1852; 
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, pp. 3404-3413; 
Jenney, C.R., Anderson, J.M., Adsorbed serum proteins responsible for surface dependent human macrophage behavior (2000) J Biomed Mater Res, 49, pp. 435-447; 
Wertz, C.F., Santore, M.M., Fibrinogen adsorption on hydrophilic and hydrophobic surfaces: geometrical and energetic aspects of interfacial relaxations (2002) Langmuir, 18, pp. 706-715; 
Pitt, W.G., Fabrizius-Homan, D.J., Mosher, D.F., Cooper, S.L., Vitronectin adsorption on polystyrene and oxidized polystyrene (1989) J Colloid Interface Sci, 129, pp. 231-239; 
Seiffert, D., Smith, J.W., The cell adhesion domain in plasma vitronectin is cryptic (1997) J Biol Chem, 272, pp. 13705-13710
},
	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.}
}
