Cross-Linking of Collagen: Endogenous aldehydes in collagen react in several ways to form a variety of unique covalent cross-links.

ML Tanzer - Science, 1973 - science.org
Science, 1973science.org
The formation of collagen cross-links is attributable to the presence of two aldehyde-
containing amino acids which react with other amino acids in collagen to generate
difunctional, trifunctional, and tetrafunctional cross-links. A necessary prerequisite for the
development of these cross-links is that the collagen molecules be assembled in the
naturally occurring fibrous polymer. Once this condition is met, cross-linking occurs in a
spontaneous, progressive fashion. The chemical structures of the cross-links dictate that …
The formation of collagen cross-links is attributable to the presence of two aldehyde-containing amino acids which react with other amino acids in collagen to generate difunctional, trifunctional, and tetrafunctional cross-links. A necessary prerequisite for the development of these cross-links is that the collagen molecules be assembled in the naturally occurring fibrous polymer. Once this condition is met, cross-linking occurs in a spontaneous, progressive fashion. The chemical structures of the cross-links dictate that very precise intermolecular alignments must occur in the collagen polymer. This seems to be a function of each specific collagen because the relative abundance of the different cross-links varies markedly, depending upon the tissue of origin of the collagen.
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