Design, synthesis, and biological evaluation of C7-functionalized DMXAA derivatives as potential human-STING agonists

Org Biomol Chem. 2019 Feb 13;17(7):1869-1874. doi: 10.1039/c8ob01798k.

Abstract

STING, a central protein in the innate immune response to cytosolic DNA, has emerged as a hot target for the development of vaccine-adjuvants and anticancer drugs. The discovery of potent human-STING (hSTING) agonist is expected to revolutionize the current cancer immunotherapy. Inspired by the X-ray crystal structure of DMXAA (5,6-dimethylxanthenone-4-acetic acid) and hSTINGG230I complex, we designed various DMXAA derivatives that contain a hydrogen bonding donor/acceptor or a halide at the C7 position. While 7-bromo- and 7-hydroxyl-DMXAA showed notable binding to mouse-STING (mSTING), our newly synthesized C7-functionalized DMXAA derivatives did not bind to hSTING. Nevertheless, our newly developed synthetic protocol for the C7-functionalization of DMXAA would be applicable to access other C7-substituted DMXAA analogues as potential hSTING agonists.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Drug Design*
  • Humans
  • Membrane Proteins / agonists*
  • Models, Molecular
  • Molecular Structure
  • Structure-Activity Relationship
  • Temperature
  • Xanthones / chemical synthesis
  • Xanthones / chemistry
  • Xanthones / pharmacology*

Substances

  • Membrane Proteins
  • STING1 protein, human
  • Xanthones
  • vadimezan