Cross-linking of collagen.
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.
D000447:Aldehydes; D000596:Amino Acids; D003094:Collagen; D008961:Models, Structural; D010455:Peptides; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D000447:Aldehydes; D000596:Amino Acids; D010455:Peptides; D003094:Collagen