Evaluation of the Inhibition of other Metalloproteinases by Matrix Metalloproteinase Inhibitors

Patrick A. Marcotte Cancer Research, Pharmaceutical Discovery Division, Abbott Laboratories, Abbott ParkIL, 60064, USACorrespondence[email protected]

Ildiko N. Elmore Cancer Research, Pharmaceutical Discovery Division, Abbott Laboratories, Abbott ParkIL, 60064, USA

Zhiwen Guan Cancer Research, Pharmaceutical Discovery Division, Abbott Laboratories, Abbott ParkIL, 60064, USA

Terrance J. Magoc Cancer Research, Pharmaceutical Discovery Division, Abbott Laboratories, Abbott ParkIL, 60064, USA

Daniel H. Albert Cancer Research, Pharmaceutical Discovery Division, Abbott Laboratories, Abbott ParkIL, 60064, USA

Douglas W. Morgan Cancer Research, Pharmaceutical Discovery Division, Abbott Laboratories, Abbott ParkIL, 60064, USA

Michael L. Curtin Cancer Research, Pharmaceutical Discovery Division, Abbott Laboratories, Abbott ParkIL, 60064, USA

Robert B. Garland Cancer Research, Pharmaceutical Discovery Division, Abbott Laboratories, Abbott ParkIL, 60064, USA

Yan Guo Cancer Research, Pharmaceutical Discovery Division, Abbott Laboratories, Abbott ParkIL, 60064, USA

H. Robin Heyman Cancer Research, Pharmaceutical Discovery Division, Abbott Laboratories, Abbott ParkIL, 60064, USA

James H. Holms Cancer Research, Pharmaceutical Discovery Division, Abbott Laboratories, Abbott ParkIL, 60064, USA

George S. Sheppard Cancer Research, Pharmaceutical Discovery Division, Abbott Laboratories, Abbott ParkIL, 60064, USA

Douglas H. Steinman Cancer Research, Pharmaceutical Discovery Division, Abbott Laboratories, Abbott ParkIL, 60064, USA

Carol K. Wada Cancer Research, Pharmaceutical Discovery Division, Abbott Laboratories, Abbott ParkIL, 60064, USA

Steven K. Davidsen Cancer Research, Pharmaceutical Discovery Division, Abbott Laboratories, Abbott ParkIL, 60064, USA

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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.

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Evaluation of the Inhibition of other Metalloproteinases by Matrix Metalloproteinase Inhibitors

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Evaluation of the Inhibition of other Metalloproteinases by Matrix Metalloproteinase Inhibitors

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