Discovery and structure-activity analysis of 4-((5-nitropyrimidin-4-yl)amino)benzimidamide derivatives as novel protein arginine methyltransferase 1 (PRMT1) inhibitors

  • Bioorg Med Chem Lett. 2015 Nov 15;25(22):5449-53. doi: 10.1016/j.bmcl.2015.06.095.
Xu-Ri Yu  1 ,  Yun Tang  2 ,  Wen-Jing Wang  1 ,  Sen Ji  1 ,  Shuang Ma  1 ,  Lei Zhong  1 ,  Chun-Hui Zhang  1 ,  Jiao Yang  1 ,  Xiao-Ai Wu  1 ,  Zheng-Yan Fu  1 ,  Lin-Li Li  3 ,  Sheng-Yong Yang  4
Affiliations
  • 1. State Key Laboratory of Biotherapy/Collaborative Innovation Center for Biotherapy, West China Hospital, West China Medical School, Sichuan University, Chengdu, Sichuan 610041, China.
  • 2. West China School of Pharmacy, Sichuan University, Chengdu, Sichuan 610041, China.
  • 3. West China School of Pharmacy, Sichuan University, Chengdu, Sichuan 610041, China. Electronic address: [email protected].
  • 4. State Key Laboratory of Biotherapy/Collaborative Innovation Center for Biotherapy, West China Hospital, West China Medical School, Sichuan University, Chengdu, Sichuan 610041, China. Electronic address: [email protected].
Abstract

Despite a potential application of PRMT1 inhibitors in Cancer treatment, very few of PRMT1 inhibitors have been reported. To obtain novel potent PRMT1 inhibitors, structure optimizations towards a hit compound, 4-((6-chloro-5-nitropyrimidin-4-yl)amino)benzimidamide, were carried out. A series of 4-((5-nitropyrimidin-4-yl)amino)benzimidamide derivatives were synthesized. Structure-activity relationship analysis led to the discovery of a number of PRMT1 inhibitors. The most potent compound corresponds to compound 6d, which showed an IC50 value of 2.0 μM against PRMT1. This compound also displayed a considerable anti-proliferative activity against three tumor cell lines, DLD-1, T24 and SH-SY-5Y, with IC50 values of 4.4 μM, 13.1 μM and 11.4 μM, respectively.

Keywords
Epigenetics; PRMT1; Protein arginine methyltransferase; Small molecule inhibitor; Structure–activity relationship.