Bacterial peptide deformylase inhibitor PMT analogs inhibit cancer cell growth by interacting with human peptide deformylase

作     者：Won-Je Kim Woo Sung Son Kyoung-Seok Ryu Seung-Kyu Lee Kwang-Hyun Choi Jong-Sun Lee Bong-Jin Lee 

作者机构：College of Pharmacy Seoul National University Seoul 151-742Korea College of Pharmacy CHA University SeongnamGyeonggi-do 487-010 Korea Division of Magnetic Resonance Korea Basic Science InstituteOchang Campus Seoul Chungcheongbuk-Do 363-883 Korea Promeditech Ltd Seoul National University Seoul 151-742Korea 

出 版 物：《Chinese Science Bulletin》 (科学通报(英文版))

年 卷 期：2014年第59卷第32期

页      面：4274-4282页

核心收录：

学科分类：1002[医学-临床医学] 100214[医学-肿瘤学] 10[医学] 

基　　金：supported by the National Research Foundation of Korea(NRF)funded by the Korean government(MEST)(2012R1A2A1A01003569&20110001207) the Korea Healthcare technology R&D Project,Ministry for Health&Welfare Affairs,Korea(A092006) supported by the Seoul Regional Small and Medium Business Administration(S1025301),in part by the 2011 BK21 project for Medicine,Dentistry,and Pharmacy 

主　　题：相互作用 抑制剂 类似物 PMT 癌细胞 类肽 细胞生长 细菌 

摘      要：Potent inhibitors of human peptide deformylase(HsPDF)were screened using known PMT analog inhibitors of bacterial peptide ***-three species of PMT analogs that are non-peptidyl bacterial PDF inhibitors like actinonin were selected using virtual screening *** species out of 43 that could bind to HsPDF were selected and their antitumor activities were *** them,four species(PMT-172,PMT-173,PMT-199,and PMT-201)showed excellent growth inhibition of cancer cell in the MTT ***-PMT binding was confirmed through a1H-CPMG-T2filter NMR experiment leading to a significant change in peak intensity for PMT-172 and *** results suggest that PMT analogs could possibly interact with HsPDF and be a novel anticancer drug candidate.