Rapid Discovery of Aspartyl Protease Inhibitors Using an Anchoring Approach

ChemMedChem. 2020 Apr 20;15(8):680-684. doi: 10.1002/cmdc.202000024. Epub 2020 Mar 18.

Abstract

Pharmacophore searches that include anchors, fragments contributing above average to receptor binding, combined with one-step syntheses are a powerful approach for the fast discovery of novel bioactive molecules. Here, we are presenting a pipeline for the rapid and efficient discovery of aspartyl protease inhibitors. First, we hypothesized that hydrazine could be a multi-valent warhead to interact with the active site Asp carboxylic acids. We incorporated the hydrazine anchor in a multicomponent reaction and created a large virtual library of hydrazine derivatives synthetically accessible in one-step. Next, we performed anchor-based pharmacophore screening of the libraries and resynthesized top-ranked compounds. The inhibitory potency of the molecules was finally assessed by an enzyme activity assay and the binding mode confirmed by several soaked crystal structures supporting the validity of the hypothesis and approach. The herein reported pipeline of tools will be of general value for the rapid generation of receptor binders beyond Asp proteases.

Keywords: MCR chemistry; aspartic protease; crystal structures; docking protocol; hydrazine-tetrazoles.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aspartic Acid Proteases / antagonists & inhibitors*
  • Aspartic Acid Proteases / metabolism
  • Drug Discovery*
  • Humans
  • Hydrazines / chemical synthesis
  • Hydrazines / chemistry
  • Hydrazines / pharmacology*
  • Molecular Structure
  • Protease Inhibitors / chemical synthesis
  • Protease Inhibitors / chemistry
  • Protease Inhibitors / pharmacology*

Substances

  • Hydrazines
  • Protease Inhibitors
  • hydrazine
  • Aspartic Acid Proteases