Understanding ligand-receptor non-covalent binding kinetics using molecular modeling

Front Biosci (Landmark Ed). 2017 Jan 1;22(6):960-981. doi: 10.2741/4527.

Abstract

Kinetic properties may serve as critical differentiators and predictors of drug efficacy and safety, in addition to the traditionally focused binding affinity. However the quantitative structure-kinetics relationship (QSKR) for modeling and ligand design is still poorly understood. This review provides an introduction to the kinetics of drug binding from a fundamental chemistry perspective. We focus on recent developments of computational tools and their applications to non-covalent binding kinetics.

Publication types

  • Review
  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Animals
  • Binding Sites
  • HIV Protease / chemistry
  • HIV Protease / metabolism
  • HIV Protease Inhibitors / pharmacokinetics
  • HIV Protease Inhibitors / pharmacology
  • Humans
  • Kinetics
  • Ligands
  • Models, Molecular
  • Molecular Dynamics Simulation
  • Polycyclic Compounds / chemistry
  • Polycyclic Compounds / metabolism
  • Protein Binding
  • Receptors, Drug / chemistry*
  • Receptors, Drug / metabolism*
  • Receptors, G-Protein-Coupled / chemistry
  • Receptors, G-Protein-Coupled / metabolism
  • Structure-Activity Relationship
  • beta-Cyclodextrins / chemistry
  • beta-Cyclodextrins / metabolism

Substances

  • HIV Protease Inhibitors
  • Ligands
  • Polycyclic Compounds
  • Receptors, Drug
  • Receptors, G-Protein-Coupled
  • beta-Cyclodextrins
  • cryptophane E
  • HIV Protease
  • p16 protease, Human immunodeficiency virus 1
  • betadex