Heterotrimeric collagen peptides as substrates of metalloproteinases

Abstract

One of main difficulties in studying the mechanism of action of collagenases and gelatinases derives from the physicochem. properties of natural collagen that is difficult to handle. Heterotrimeric collagenous peptides contg. the collagenase cleavage site 772-784 (P4-P'9)/772-785 (P4-P'10) of the two α1 chains and 772-784 (P4-P'9) of the α2 chain of collagen type I were assembled in the α1/α2/α1' register and stabilized in their triple-helical fold with a modeled C-terminal cystine knot and N-terminally by (Gly-Pro-Hyp)n extensions of increasing chain length. The order of chain assembly corresponds to the register proposed for collagen type I on the basis of theor. considerations. [on SciFinder(R)]