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Influence of the telopeptides on type I collagen fibrillogenesis
Author(s) -
Brennan Maureen,
Davison Peter F.
Publication year - 1981
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1981.360201012
Subject(s) - cyanogen bromide , fibrillogenesis , chemistry , fibril , type i collagen , proteolysis , in vitro , biochemistry , biophysics , peptide sequence , enzyme , endocrinology , medicine , biology , gene
Preparations have been made of acid‐soluble collagens whose telopeptides have suffered different levels of proteolytic attack. The collagens with more intact telopeptides form fibrils more rapidly than those with degraded telopeptides. In addition, we have shown that a high molecular weight aggregate rich in the carboxyterminal CNBr peptide, α1CB6, can be found in cyanogen bromide digests of fibrils formed from intact collagen. A similar aggregate is found in CNBr digests of native tendons. The aggregate formed in fibrils assembled in vitro can be stabilized by reduction, and its generation is strongly dependent on the presence of intact telopeptides. The latter point is the most objective evidence that to reproduce the characteristics of native fibrils in vitro , the collagen telopeptides must be preserved from proteolysis.