Structure-based drug design, synthesis and biological assays of P. falciparum Atg3-Atg8 protein-protein interaction inhibitors

J Comput Aided Mol Des. 2018 Mar;32(3):473-486. doi: 10.1007/s10822-018-0102-5. Epub 2018 Jan 30.

Abstract

The proteins involved in the autophagy (Atg) pathway have recently been considered promising targets for the development of new antimalarial drugs. In particular, inhibitors of the protein-protein interaction (PPI) between Atg3 and Atg8 of Plasmodium falciparum retarded the blood- and liver-stages of parasite growth. In this paper, we used computational techniques to design a new class of peptidomimetics mimicking the Atg3 interaction motif, which were then synthesized by click-chemistry. Surface plasmon resonance has been employed to measure the ability of these compounds to inhibit the Atg3-Atg8 reciprocal protein-protein interaction. Moreover, P. falciparum growth inhibition in red blood cell cultures was evaluated as well as the cyto-toxicity of the compounds.

Keywords: 1,2,3-Triazole; Atg8 inhibitors; Autophagy; Docking; Malaria; PPI inhibitors; Peptidomimetics.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antimalarials / chemistry*
  • Antimalarials / pharmacology
  • Autophagy
  • Autophagy-Related Proteins / antagonists & inhibitors*
  • Cell Survival / drug effects
  • Drug Design
  • Hep G2 Cells
  • Humans
  • Molecular Docking Simulation
  • Molecular Dynamics Simulation
  • Peptidomimetics / chemical synthesis*
  • Peptidomimetics / pharmacology
  • Plasmodium falciparum / drug effects
  • Protein Binding
  • Protozoan Proteins / antagonists & inhibitors*
  • Structure-Activity Relationship
  • Triazoles / chemical synthesis*
  • Triazoles / pharmacology

Substances

  • Antimalarials
  • Autophagy-Related Proteins
  • Peptidomimetics
  • Protozoan Proteins
  • Triazoles