Discovery of a potent and dual-selective bisubstrate inhibitor for protein arginine methyltransferase 4/5.
10.1016/j.apsb.2020.10.013
- Author:
Ayad A AL-HAMASHI
1
;
Dongxing CHEN
1
;
Youchao DENG
1
;
Guangping DONG
1
;
Rong HUANG
1
Author Information
1. Department of Medicinal Chemistry and Molecular Pharmacology, Center for Cancer Research, Institute for Drug Discovery, Purdue University, West Lafayette, IN 47907, USA.
- Publication Type:Journal Article
- Keywords:
Bisubstrate analogue;
Bisubstrate inhibitor;
GAR, glycine and arginine;
IC50, half-maximal inhibition concentration;
NTMTs, N-terminal methyltransferases;
PKMTs, protein lysine methyltransferases;
PRMTs, protein arginine methyltransferases;
Protein arginine methyltransferase;
Protein arginine methyltransferase 4;
Protein arginine methyltransferase 5;
SAH, S-(5′-adenosyl)-l-homocysteine;
SAM, S-adenosylmethionine;
SNF, sinofungin;
TLC, thin-layer chromatography
- From:
Acta Pharmaceutica Sinica B
2021;11(9):2709-2718
- CountryChina
- Language:English
-
Abstract:
Protein arginine methyltransferases (PRMTs) have been implicated in the progression of many diseases. Understanding substrate recognition and specificity of individual PRMT would facilitate the discovery of selective inhibitors towards future drug discovery. Herein, we reported the design and synthesis of bisubstrate analogues for PRMTs that incorporate a
