Selectivity of inhibition of matrix metalloproteases MMP-3 and MMP-2 by succinyl hydroxamates and their carboxylic acid analogues is dependent on P3' group chirality

Bioorg Med Chem Lett. 2001 Feb 26;11(4):567-70. doi: 10.1016/s0960-894x(00)00719-8.

Abstract

Structure-activity relationships are described for a series of succinyl hydroxamic acids 1a-o and their carboxylic acid analogues 2a-o as inhibitors of matrix metalloproteases MMP-3 and MMP-2. For this series (P1' = (CH2)3Ph, P2' = t-Bu) selectivity for the inhibition of MMP-2 was found to be strongly dependent on P3'.

MeSH terms

  • Hydroxamic Acids / pharmacology*
  • Matrix Metalloproteinase Inhibitors*
  • Protease Inhibitors / chemical synthesis
  • Protease Inhibitors / pharmacology*
  • Structure-Activity Relationship

Substances

  • Hydroxamic Acids
  • Matrix Metalloproteinase Inhibitors
  • Protease Inhibitors