Matrix metalloproteinase inhibitors: A structure-activity study

Daniel E. Levy*, France Lapierre, Weisheng Liang, Wenqing Ye, Christopher W. Lange, Xiaoyuan Li, Damian Grobelny, Marie Casabonne, David Tyrrell, Kevin Holme, Alex Nadzan, Richard E. Galardy

*Corresponding author for this work

Research output: Contribution to journalJournal Articlepeer-review

164 Citations (Scopus)

Abstract

Modifications around the dipeptide-mimetic core of a hydroxamic acid based matrix metalloproteinase inhibitor were studied. These variations incorporated a variety of natural, unnatural, and synthetic amino acids inaddition to modifications of the P1' and P3' substituents. The results of this study indicate the following structural requirements: (2) Potent inhibitorsmust possess string zinc-binding functionalities. (3) The potential importance of the hydrophobic group at position R3 as illustratedby itsability to impart greater relative potency against stromelysin when larger hydrophobic groups are used. (4) Requirements surrounding the nature of the amino acid appear to be more restrictive for stromelysin than for neutrophil collagenase, 72 kDa gelatinase, and 92 kDa gelatinase. These requirements may involve planar fused-ring aryl systems and possibly hydrogen-bonding capabilities.

Original languageEnglish
Pages (from-to)199-223
Number of pages25
JournalJournal of Medicinal Chemistry
Volume41
Issue number2
DOIs
Publication statusPublished - 1998
Externally publishedYes

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