Inhibition of matrix metalloproteinases by peptidyl hydroxamic acids.


Synthetic inhibitors of interstitial collagenase, tri- and tetrapeptidyl hydroxamic acids, have been developed and tested for their inhibitory activities against human matrix metalloproteinases. A water soluble inhibitor, p-NH2-Bz-Gly-Pro-D-Leu-D-Ala-NHOH (FN-439) inhibited interstitial and granulocyte collagenases, granulocyte gelatinase and skin fibroblast stromelysin with IC50 of 1 x 10(-6) M, 3.0 x 10(-5) M and 1.5 x 10(-4), respectively, but not thermolysin and serine proteinases. FN-439 was found to retain its inhibitory activity against matrix metalloproteinases even after prolonged incubation with pronase or human granulocyte elastase, indicating a favorite candidate of the inhibitor to modulate metalloproteinase activities in vivo.

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@article{Odake1994InhibitionOM, title={Inhibition of matrix metalloproteinases by peptidyl hydroxamic acids.}, author={Shinjiro Odake and Yusuke Morita and Toshiaki Morikawa and Norimasa Yoshida and Hitoshi Hori and Yusuke Nagai}, journal={Biochemical and biophysical research communications}, year={1994}, volume={199 3}, pages={1442-6} }