Affinity-Based Protein Profiling Reveals Cellular Targets of Photoreactive Anticancer Inhibitors

ACS Chem Biol. 2019 Dec 20;14(12):2546-2552. doi: 10.1021/acschembio.9b00784. Epub 2019 Nov 26.

Abstract

Affinity-based protein profiling has proven to be a powerful method in target identification of bioactive molecules. Here, this technology was applied in two photoreactive anticancer inhibitors, arenobufagin and HM30181. Using UV irradiation, these photoreactive reagents can covalently cross-link to target proteins, leading to a covalent binding with target proteins. Moreover, the cellular on/off targets of these two molecules, including ATP1A1, MDR1, PARP1, DDX5, NOP2, RAB6A, and ERGIC1 were first identified by affinity-based protein profiling and bioimaging approaches. The protein hit, PARP1, was further validated to be involved in the function of the anticancer effects.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antineoplastic Agents / pharmacology*
  • HeLa Cells
  • Hep G2 Cells
  • Humans
  • Light*
  • Photoaffinity Labels
  • Proteins / metabolism*
  • Ultraviolet Rays

Substances

  • Antineoplastic Agents
  • Photoaffinity Labels
  • Proteins