Targeted Protein Degradation via a Covalent Reversible Degrader Based on Bardoxolone

02 April 2020, Version 1
This content is a preprint and has not undergone peer review at the time of posting.

Abstract

Targeted protein degradation (TPD) has emerged as a powerful tool in drug discovery for the perturbation of protein levels using heterobifunctional small molecules (i.e. PROTACs). E3 ligase recruiters remain central to this process yet relatively few have been identified relative to the >500 predicted human E3 ligases. While, initial recruiters have utilized non-covalent chemistry for protein binding, very recently covalent engagement to novel E3’s has proven fruitful in TPD application. Herein we demonstrate efficient proteasome-mediated degradation of BRD4 by a bifunctional small molecule linking the KEAP1-NRF2 activator bardoxolone to a BRD4 inhibitor JQ1. Notably, this work reports the first covalent, reversible E3 ligase recruiter for TPD applications.

Keywords

CDDO
bardoxolone methyl
KEAP1
NRF2
PROTAC
degrader
targeted protein degradation
E3 ligase
cysteine
BRD4

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