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

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.