Asymmetric synthesis and evaluation of epoxy-α-acyloxycarboxamides as selective inhibitors of cathepsin L

Bioorg Med Chem. 2017 Sep 1;25(17):4620-4627. doi: 10.1016/j.bmc.2017.06.048. Epub 2017 Jun 29.

Abstract

Cathepsin L plays important roles in physiological processes as well as in the development of many pathologies. Recently the attentions were turned to its association with tumor progress what makes essential the development of more potent and selective inhibitors. In this work, epoxipeptidomimetics were investigated as new cathepsin inhibitors. This class of compounds is straightforward obtained by using a green one-pot asymmetric epoxidation/Passerini 3-MCR. A small library of 17 compounds was evaluated against cathepsin L, and among them LSPN423 showed to be the most potent. Investigations of the mechanism suggested a tight binding uncompetitive inhibition.

Keywords: Cathepsin L inhibitor; Epoxipeptidomimetics; Green synthesis; Tight binding inhibitor.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amides / chemistry*
  • Amides / metabolism
  • Amides / pharmacology
  • Animals
  • Antiparasitic Agents / chemistry
  • Antiparasitic Agents / metabolism
  • Antiparasitic Agents / pharmacology
  • Cathepsin L / antagonists & inhibitors*
  • Cathepsin L / metabolism
  • Cysteine Proteinase Inhibitors / chemical synthesis*
  • Cysteine Proteinase Inhibitors / metabolism
  • Cysteine Proteinase Inhibitors / pharmacology
  • Inhibitory Concentration 50
  • Parasites / drug effects
  • Parasites / enzymology
  • Stereoisomerism
  • Structure-Activity Relationship

Substances

  • Amides
  • Antiparasitic Agents
  • Cysteine Proteinase Inhibitors
  • Cathepsin L