Abstract
The hierarchical self-assembly of collagen type II, the major fibril-forming collagen of cartilage, has been studied by atomic force microscopy (AFM). The fibrillation of human collagen type II in simulated body fluid (SBF) was investigated by varying the incubation time, pH, and temperature as well as the collagen concentration. The results reveal that the collagen type II fibrillogenesis process from procollagen into D-banded fibrils is entropy driven, and that incubation at low temperature leads to the formation of distinct hierarchical supramolecular assemblies.
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