文献类型：期刊文献

英文题名：Host defense peptide mimicking cyclic peptoid polymers exerting strong activity against drug-resistant bacteria

作者：Zhang, Wenjing[1];Deng, Shuai[1];Zhou, Min[1];Zou, Jingcheng[2];Xie, Jiayang[2];Xiao, Ximian[2];Yuan, Ling[2];Ji, Zhemin[2];Chen, Sheng[2];Cui, Ruxin[2];Luo, Zhengjie[2];Xia, Guixue[2];Liu, Runhui[1,2]

机构：[1]East China Univ Sci & Technol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China;[2]East China Univ Sci & Technol, Frontiers Sci Ctr Materiobiol & Dynam Chem, Sch Mat Sci & Engn,Shanghai Frontiers Sci Ctr Opt, Res Ctr Biomed Mat,Minist Educ,Key Lab Ultrafine, Shanghai 200237, Peoples R China

年份：2022

卷号：10

期号：16

起止页码：4515

外文期刊名：BIOMATERIALS SCIENCE

收录：;EI(收录号：20223712716056);WOS:【SCI-EXPANDED(收录号:WOS:000820720300001)】；

基金：This research was supported by the National Natural Science Foundation of China (No. 22075078, 21861162010), National Postdoctoral Program for Innovative Talents (BX2021102), Program of Shanghai Academic/Technology Research Leader (20XD1421400), Shanghai Sailing Program (Grant Number: 21YF1409100), and the Frontier Science Research Base of Optogenetic Techniques for Cell Metabolism grant 2021 Sci & Tech 03-28 (Shanghai Municipal Education Commission). We thank the staff members of the Mass Spectrometry System at the National Facility for Protein Science in Shanghai (NFPS), Zhangjiang Lab, China for providing technical support and assistance in data collection and analysis. We also thank the Research Center of Analysis and Test of East China University of Science and Technology for the help with the characterization.

语种：英文

外文关键词：Amino acids - Bacteria - Network security

摘要：Extensive use of antibiotics accelerates the emergence of drug-resistant bacteria and related infections. Host defense peptides (HDPs) have been studied as promising and potential therapeutic candidates. However, their clinical applications of HDPs are limited due to their high cost of synthesis and low stability upon proteolysis. Therefore, HDP mimics have become a new approach to address the challenge of bacterial resistance. In this work, we design the amphiphilic peptoid polymers by mimicking the positively charged and hydrophobic structures of HDPs and synthesize a series of cyclic peptoid polymers efficiently via the polymerization on alpha-amino acid N-substituted glycine N-carboxyanhydrides (alpha-NNCAs) using 1,8-diazabicycloundec-7-ene (DBU) as the initiator. The optimal cyclic peptoid polymer, poly(Naeg(0.7)Npfbg(0.3))(20), displays strong antibacterial activities against drug-resistant bacteria, but low hemolysis and cytotoxicity. In addition, the mode-of-action study indicates that the antibacterial mechanism is associated with bacterial membrane interaction. Our study implies that HDP mimicking cyclic peptoid polymers have potential application in treating drug-resistant bacterial infections.