Design, Synthesis, and Biological Evaluation of Retinoic Acid-Related Orphan Receptor γt (RORγt) Agonist Structure-Based Functionality Switching Approach from In House RORγt Inverse Agonist to RORγt Agonist

J Med Chem. 2019 Feb 14;62(3):1167-1179. doi: 10.1021/acs.jmedchem.8b01181. Epub 2019 Feb 4.

Abstract

Retinoic acid receptor-related orphan receptor γt (RORγt) agonists are expected to provide a novel class of immune-activating anticancer drugs via activation of Th17 cells and Tc17 cells. Herein, we describe a novel structure-based functionality switching approach from in house well-optimized RORγt inverse agonists to potent RORγt agonists. We succeeded in the identification of potent RORγt agonist 5 without major chemical structure change. The biochemical response was validated by molecular dynamics simulation studies that showed a helix 12 stabilization effect of RORγt agonists. These results indicate that targeting helix 12 is an attractive and novel medicinal chemistry strategy for switching existing RORγt inverse agonists to agonists.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Drug Design*
  • Drug Inverse Agonism*
  • High-Throughput Screening Assays
  • Molecular Dynamics Simulation
  • Nuclear Receptor Subfamily 1, Group F, Member 3 / agonists*
  • Structure-Activity Relationship
  • Th17 Cells / drug effects

Substances

  • Nuclear Receptor Subfamily 1, Group F, Member 3
  • RORC protein, human