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Zinc is likely a cofactor for 2 kinds of cross-linking interactions; one involving direct binding between laminin and collagen type IV and the other a ternary complex of laminin-entactin-collagen type IV.
The results of this study suggest that most of the zinc atoms detected were attached to hydroxyapatite and not to collagen.
Neither inhibition of polysomal protein synthesis nor increased degradation of mature collagen fibers was found to play any major role in the effect of zinc.
To our knowledge, this is the first report on cyclic phosphinic peptides and on their activities as inhibitors of a zinc protease.
Zinc can prevent collagen hydrolysis by MMPs.

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