Toward Understanding the Structural Basis of Partial Agonism at the Dopamine D3 Receptor

J Med Chem. 2017 Jan 26;60(2):580-593. doi: 10.1021/acs.jmedchem.6b01148. Epub 2017 Jan 5.

Abstract

Both dopamine D3 receptor (D3R) partial agonists and antagonists have been implicated as potential medications for substance use disorders. In contrast to antagonists, partial agonists may cause fewer side effects since they maintain some dopaminergic tone and may be less disruptive to normal neuronal functions. Here, we report three sets of 4-phenylpiperazine stereoisomers that differ considerably in efficacy: the (R)-enantiomers are antagonists/weak partial agonists, whereas the (S)-enantiomers are much more efficacious. To investigate the structural basis of partial agonism, we performed comparative microsecond-scale molecular dynamics simulations starting from the inactive state of D3R in complex with these enantiomers. Analysis of the simulation results reveals common structural rearrangements near the ligand binding site induced by the bound (S)-enantiomers, but not by the (R)-enantiomers, that are features of partially activated receptor conformations. These receptor models bound with partial agonists may be useful for structure-based design of compounds with tailored efficacy profiles.

Publication types

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

MeSH terms

  • Binding Sites
  • Drug Partial Agonism
  • HEK293 Cells
  • Humans
  • Molecular Dynamics Simulation
  • Piperazines / chemical synthesis
  • Piperazines / chemistry
  • Piperazines / pharmacology*
  • Protein Structure, Tertiary
  • Receptors, Dopamine D3 / agonists*
  • Receptors, Dopamine D3 / chemistry*
  • Stereoisomerism

Substances

  • Piperazines
  • Receptors, Dopamine D3