Factors and mechanisms determining the formation of fibrillar collagen structures in adsorbed phases

被引:34
作者
Gurdak, Elzbieta [1 ]
Rouxhet, Paul G. [1 ]
Dupont-Gillain, Christine C. [1 ]
机构
[1] Catholic Univ Louvain, Unite Chim Interfaces, B-1348 Louvain, Belgium
关键词
polystyrene; collagen; adsorption; collagen adsorption; collagen aggregation; atomic force microscopy (AFM); x-ray photoelectron spectroscopy (XPS);
D O I
10.1016/j.colsurfb.2006.07.011
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
The adsorption of collagen (type I from calf skin) was studied, comparing different collagen sources and using substrates which differ according to surface hydrophobicity (polystyrene, either native, with OH substitution of each repeat unit, with COOH substitution of a small fraction of repeat units, or surface modified by oxygen plasma discharge). The atomic force microscopy observation of the adsorbed layers showed that aggregation in the solution acts in competition with the formation of fibrils in the adsorbed phase; more aggregated solutions behave like less concentrated solutions regarding adsorption. The fibrils formed in the adsorbed phase are much smaller than the fibrils formed in the suspension, and, in contrast with the latter, do not show regular band pattern. It is confirmed that fibrils formation occurs more readily on more hydrophobic surfaces, which is tentatively attributed to a greater mobility of individual molecules adsorbed on more hydrophobic substrates. This interpretation is supported by previously published radiochemical measurements. However, the comparison of strongly different adsorption procedures (progressive on the one hand; quick and massive on the other hand) did not provide any additional clue. (c) 2006 Elsevier B.V. All rights reserved.
引用
收藏
页码:76 / 88
页数:13
相关论文
共 48 条
[1]  
[Anonymous], 1984, ULTRASTRUCT CONNECT, DOI DOI 10.1007/978-1-4613-2831-5_1
[3]  
BASZKIN A, 1987, ACS SYM SER, V343, P451
[4]   The collagen triple-helix structure [J].
Brodsky, B ;
Ramshaw, JAM .
MATRIX BIOLOGY, 1997, 15 (8-9) :545-554
[5]   Procollagen trafficking, processing and fibrillogenesis [J].
Canty, EG ;
Kadler, KE .
JOURNAL OF CELL SCIENCE, 2005, 118 (07) :1341-1353
[6]  
CHANDRAKASAN G, 1976, J BIOL CHEM, V251, P6062
[7]   Nanoscale organization of collagen and mixed collagen-pluronic adsorbed layers [J].
De Cupere, VM ;
Van Wetter, J ;
Rouxhet, PG .
LANGMUIR, 2003, 19 (17) :6957-6967
[8]   Protein adsorption on model surfaces with controlled nanotopography and chemistry [J].
Denis, FA ;
Hanarp, P ;
Sutherland, DS ;
Gold, J ;
Mustin, C ;
Rouxhet, PG ;
Dufrêne, YF .
LANGMUIR, 2002, 18 (03) :819-828
[9]   Influence of substrate hydrophobicity on the adsorption of collagen in the presence of pluronic F68, albumin, or calf serum [J].
Dewez, JL ;
Berger, V ;
Schneider, YJ ;
Rouxhet, PG .
JOURNAL OF COLLOID AND INTERFACE SCIENCE, 1997, 191 (01) :1-10
[10]   Competitive adsorption of proteins: Key of the relationship between substratum surface properties and adhesion of epithelial cells [J].
Dewez, JL ;
Doren, A ;
Schneider, YJ ;
Rouxhet, PG .
BIOMATERIALS, 1999, 20 (06) :547-559