Evaluation of the Inhibition of other Metalloproteinases by Matrix Metalloproteinase Inhibitors
- 1 January 1999
- journal article
- research article
- Published by Taylor & Francis in Journal of Enzyme Inhibition
- Vol. 14 (6) , 425-435
- https://doi.org/10.3109/14756369909030333
Abstract
Two series of compounds synthesized as specific matrix metalloproteinase (MMP) inhibitors have been evaluated for their inhibition of non-MMPs. In a series of substituted succinyl hydrox-amic acids, some were found to be significant (IC50 < 1 μM) inhibitors of leucine (microsomal) aminopeptidase, neprilysin (3.4.24.11), and thermolysin. Macrocyclic compounds in which the alpha carbon of the succinyl hydroxamate is linked to the side chain of the P2′ amino acid were found to be good inhibitors of aminopeptidase, but not of neprilysin or themolysin. Compounds of neither series were found to be significant inhibitors of angiotensin converting enzyme or carboxypeptidase A.Keywords
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