Cell adhesion peptide modification of gold-coated polyurethanes for vascular endothelial cell adhesion

被引:0
作者
McMillan, R
Meeks, B
Bensebaa, F
Deslandes, Y
Sheardown, H
机构
[1] McMaster Univ, Dept Chem Engn, Hamilton, ON L8S 4L7, Canada
[2] Univ Ottawa, Dept Chem Engn, Ottawa, ON K1N 6N5, Canada
[3] Natl Res Council Canada, ICPET, Ottawa, ON K1A 0R6, Canada
来源
JOURNAL OF BIOMEDICAL MATERIALS RESEARCH | 2001年 / 54卷 / 02期
关键词
surface modification; cell-adhesion peptide; gold-thiol chemistry; vascular endothelial cells;
D O I
10.1002/1097-4636(200102)54:2<272::AID-JBM15>3.0.CO;2-3
中图分类号
R318 [生物医学工程];
学科分类号
0831 ;
摘要
Gold-coated polyurethanes were chemisorbed with three cell-adhesion peptides having an N-terminal cysteine: cys-arg-gly-asp (CRGD), cys-arg-glu-asp-val (CREDV), and the cyclic peptide cys-cys-arg-arg-gly-asp-try-leu-cys (CCRRGDWLC). The peptides were selected based on their presumed preferential interactions with the cell-surface integrins on vascular endothelial cells. The ability of the surfaces to support the preferential adhesion of human vascular endothelial cells was studied by comparing in vitro adhesion results for these cells with those from mouse 3T3 fibroblasts. Surface modification with the peptides was confirmed by water-contact angles and XPS. Surface morphology was determined by AFM and SEM. In vitro cell-culture studies in conjunction with plasma-protein adsorption and immunoblotting were performed on the various modified surfaces. The data suggest that peptide-modified surfaces have significant potential for supporting cell adhesion. Little or no cell adhesion was noted on gold- or cysteine-modified control surfaces. Human vascular endothelial cells showed the greatest adhesion to the CCRRG-DWLC-modified surfaces, and the 3T3 fibroblasts adhered best to the CREDV-modified surfaces. Protein adsorption studies suggest that the preferential adsorption of the cell-adhesive proteins fibronectin and vitronectin is not likely mediating the differences noted. It is concluded that the cell-adhesive peptide-modified gold-coated polymers have significant potential for further development both as model substrates for fundamental studies and for use in biomaterials applications. (C) 2000 John Wiley & Sons, Inc.
引用
收藏
页码:272 / 283
页数:12
相关论文
共 41 条
[1]   FORMATION OF MONOLAYER FILMS BY THE SPONTANEOUS ASSEMBLY OF ORGANIC THIOLS FROM SOLUTION ONTO GOLD [J].
BAIN, CD ;
TROUGHTON, EB ;
TAO, YT ;
EVALL, J ;
WHITESIDES, GM ;
NUZZO, RG .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1989, 111 (01) :321-335
[2]   MOLECULAR-LEVEL CONTROL OVER SURFACE ORDER IN SELF-ASSEMBLED MONOLAYER FILMS OF THIOLS ON GOLD [J].
BAIN, CD ;
WHITESIDES, GM .
SCIENCE, 1988, 240 (4848) :62-63
[3]   Kinetics of formation of long-chain n-alkanethiolate monolayers on polycrystalline gold [J].
Bensebaa, F ;
Voicu, R ;
Huron, L ;
Ellis, TH ;
Kruus, E .
LANGMUIR, 1997, 13 (20) :5335-5340
[4]  
Bensebaa F, 1998, SURF SCI, V405, pL472
[5]   INFRARED STUDY OF THIOL MONOLAYER ASSEMBLIES ON GOLD - PREPARATION, CHARACTERIZATION, AND FUNCTIONALIZATION OF MIXED MONOLAYERS [J].
BERTILSSON, L ;
LIEDBERG, B .
LANGMUIR, 1993, 9 (01) :141-149
[6]  
BRADLEY BK, 1988, ANAL BIOCHEM, V172, P270
[7]   X-ray photoelectron spectroscopy sulfur 2p study of organic thiol and disulfide binding interactions with gold surfaces [J].
Castner, DG ;
Hinds, K ;
Grainger, DW .
LANGMUIR, 1996, 12 (21) :5083-5086
[8]   MOLECULAR ORDER AT THE SURFACE OF AN ORGANIC MONOLAYER STUDIED BY LOW-ENERGY HELIUM DIFFRACTION [J].
CHIDSEY, CED ;
LIU, GY ;
ROWNTREE, P ;
SCOLES, G .
JOURNAL OF CHEMICAL PHYSICS, 1989, 91 (07) :4421-4423
[9]   IDENTIFICATION OF PROTEINS ADSORBED TO HEMODIALYZER MEMBRANES FROM HEPARINIZED PLASMA [J].
CORNELIUS, RM ;
BRASH, JL .
JOURNAL OF BIOMATERIALS SCIENCE-POLYMER EDITION, 1993, 4 (03) :291-304
[10]   WETTING AND PROTEIN ADSORPTION OF SELF-ASSEMBLED MONOLAYERS OF ALKANETHIOLATES SUPPORTED ON TRANSPARENT FILMS OF GOLD [J].
DIMILLA, PA ;
FOLKERS, JP ;
BIEBUYCK, HA ;
HARTER, R ;
LOPEZ, GP ;
WHITESIDES, GM .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1994, 116 (05) :2225-2226