Intermolecular Cross‐Links of Collagen

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Abstract
The present communication provides experimental proof for involvement in intermolecular cross‐links of the nonhelical area at the carboxy‐terminal end of the α1‐chain of collagen. Compared to soluble collagen, the content of α1‐CB6, the carboxy‐terminal peptide of the α1‐chain, was significantly low in cyanogen bromide digests of highly cross‐linked insoluble collagen from calf achilles tendon collagen. Approximately 50% of the α1‐CB6 could be identified by serological techniques within a peptide fraction of molecular weight approximately 50000. In this fraction, α1‐CB6 was thought to be cross‐linked by intermolecular bonds to certain cyanogen bromide peptides, i.e.α1‐CB7, α1‐CB8 and α2‐CB4. These intermolecular bonds were cleaved by brief pepsin treatment such that free α1‐CB6 was liberated by subsequent cyanogen bromide digestion. On the basis of the amino acid sequence of the α1‐chain presently known and the arrangement of the collagen within the fibrils, putative cross‐link regions were identified within the helical area which may cross‐link with lysine‐derived aldehydes present in the nonhelical amino‐ and carboxy‐terminal areas of adjacent molecules.

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