Water envelope has a critical impact on the design of protein-protein interaction inhibitors

Chem Commun (Camb). 2020 Apr 21;56(31):4360-4363. doi: 10.1039/c9cc07714f. Epub 2020 Mar 20.

Abstract

We show that a water envelope network plays a critical role in protein-protein interactions (PPI). The potency of a PPI inhibitor is modulated by orders of magnitude on manipulation of the solvent envelope alone. The structure-activity relationship of PEX14 inhibitors was analyzed as an example using in silico and X-ray data.

MeSH terms

  • Computer Simulation
  • Crystallography, X-Ray
  • Humans
  • Membrane Proteins / chemistry
  • Membrane Proteins / metabolism*
  • Molecular Structure
  • Peroxisome-Targeting Signal 1 Receptor / metabolism
  • Proof of Concept Study
  • Protein Binding / drug effects
  • Protein Multimerization / drug effects*
  • Protozoan Proteins / chemistry
  • Protozoan Proteins / metabolism*
  • Pyrazoles / chemistry*
  • Pyrrolidines / chemistry*
  • Structure-Activity Relationship
  • Trypanosoma brucei brucei / chemistry
  • Water / chemistry
  • Water / metabolism*

Substances

  • Membrane Proteins
  • PEX14 protein, Trypanosoma brucei
  • PEX5 protein, human
  • Peroxisome-Targeting Signal 1 Receptor
  • Protozoan Proteins
  • Pyrazoles
  • Pyrrolidines
  • Water