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Temporal Assembly of Collagen Type II Studied by Atomic Force Microscopy
Author(s) -
Dong M.,
Xu S.,
Bünger M. H.,
Birkedal H.,
Besenbacher F.
Publication year - 2007
Publication title -
advanced engineering materials
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.938
H-Index - 114
eISSN - 1527-2648
pISSN - 1438-1656
DOI - 10.1002/adem.200700220
Subject(s) - fibrillogenesis , fibril , atomic force microscopy , procollagen peptidase , type i collagen , biophysics , materials science , collagen fibril , incubation , crystallography , chemistry , nanotechnology , biochemistry , biology , microbiology and biotechnology , endocrinology
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.