Peptide hydroxamic acids inhibit skin collagenase.
A number of peptide hydroxamic acids have been synthesized and have been shown to be inhibitors of human skin collagenase. One of these, Z-Pro-Leu-Gly-NHOH, has an IC50 value of 4 X 10(-5)M. Corresponding peptides with different C-terminal functional groups, such as amide, carboxylate and aldehyde, showed little or no inhibition, indicating the importance of the hydroxamate functional group. In addition, the peptide sequence of this effective inhibitor corresponds closely to that of the cleavage site of native collagen, the substrate for the enzyme. Thus, substrate analogs incorporating a suitable metal coordinating group serve as potential inhibitors of human collagenase.
D000900:Anti-Bacterial Agents; D002216:Captopril / Q000494:pharmacology; D010450:Endopeptidases; D005347:Fibroblasts / Q000201:enzymology; D006801:Humans; D006877:Hydroxamic Acids / Q000494:pharmacology*; D008666:Metalloendopeptidases; D003012:Microbial Collagenase / Q000037:antagonists & inhibitors*; D009842:Oligopeptides / Q000494:pharmacology; D010455:Peptides; D011480:Protease Inhibitors; D012867:Skin / Q000201:enzymology*
D000900:Anti-Bacterial Agents; D006877:Hydroxamic Acids; D009842:Oligopeptides; D010455:Peptides; D011480:Protease Inhibitors; C016977:amastatin; C048727:zincov; D002216:Captopril; D010450:Endopeptidases; D008666:Metalloendopeptidases; D003012:Microbial Collagenase