兰州大学机构库
Antimicrobial peptides with symmetric structures against multidrug-resistant bacteria while alleviating antimicrobial resistance
Zhong, Chao1,2; Zhang, Fangyan2; Yao, Jia4; Zhu, Yuewen2; Zhu, Ningyi2; Zhang, Yun2; Liu, Hui2; Gou, Sanhu2; Ni, Jingman1,2,3
2021-04
Online publication date2021-03
Source PublicationBIOCHEMICAL PHARMACOLOGY   Impact Factor & Quartile
ISSN0006-2952
EISSN1873-2968
Volume186
page numbers25
AbstractIn response to the dramatically increasing antimicrobial resistance, a series of new symmetric peptides were designed and synthesized in this study by a ?WWW? motif as the symmetric center, arginine as the positive charge amino acid and the terminus symmetrically tagged with hydrophobic amino acids. Amongst the new symmetric peptide FRRW (FRRWWWRRF-NH2) presented the highest cell selectivity for bacteria over mammalian cell and exerted excellent antimicrobial potential against a broad of bacteria, especially difficult-tokill multidrug-resistant strains clinical isolates. FRRW also displayed perfect stability in physiological salt ions and rapid killing speed as well as acted on multiple mechanisms including non-receptor mediated membrane and intra-molecular mechanisms. Importantly, FRRW emerged a low tendency of resistance in contrast to traditional antibiotics ciprofloxacin and gentamicin. What?s more, FRRW could resist or alleviate or even reverse the ciprofloxacin- and gentamicin-resistance by changing the permeability of bacterial membrane and inhibiting the efflux pumps of bacteria. Furthermore, FRRW exhibited remarkable effectiveness and higher safety in vivo than polymyxin B. In summary, the new symmetric peptide FRRW was promised to be as a new antimicrobial candidate for overcoming the increasing bacterial resistance.
KeywordAntimicrobial peptidesAntimicrobial activityAnti-resistanceMultidrug-resistant bacteriaBiocompatibilityMultiple mechanisms
PublisherPERGAMON-ELSEVIER SCIENCE LTD
DOI10.1016/j.bcp.2021.114470
Indexed BySCOPUS ; SCIE
Language英语
WOS Research AreaPharmacology & Pharmacy
WOS SubjectPharmacology & Pharmacy
WOS IDWOS:000640414700001
Original Document TypeArticle
PMID 33610592
Citation statistics
Cited Times:17[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttps://ir.lzu.edu.cn/handle/262010/450387
Collection兰州大学
Corresponding AuthorNi, Jingman
Affiliation
1.Lanzhou Univ, Sch Basic Med Sci, Key Lab Preclin Study New Drugs Gansu Prov, Lanzhou 730000, Peoples R China;
2.Lanzhou Univ, Sch Pharm, Lanzhou 730000, Peoples R China;
3.Macau Univ Sci & Technol, State Key Lab Qual Res Chinese Med, Ave Wai Long, Taipa 999078, Macao, Peoples R China;
4.Lanzhou Univ, Hosp 1, Lanzhou 730000, Peoples R China
Recommended Citation
GB/T 7714
Zhong, Chao,Zhang, Fangyan,Yao, Jia,et al. Antimicrobial peptides with symmetric structures against multidrug-resistant bacteria while alleviating antimicrobial resistance[J]. BIOCHEMICAL PHARMACOLOGY,2021,186.
APA Zhong, Chao.,Zhang, Fangyan.,Yao, Jia.,Zhu, Yuewen.,Zhu, Ningyi.,...&Ni, Jingman.(2021).Antimicrobial peptides with symmetric structures against multidrug-resistant bacteria while alleviating antimicrobial resistance.BIOCHEMICAL PHARMACOLOGY,186.
MLA Zhong, Chao,et al."Antimicrobial peptides with symmetric structures against multidrug-resistant bacteria while alleviating antimicrobial resistance".BIOCHEMICAL PHARMACOLOGY 186(2021).
Files in This Item:
There are no files associated with this item.
Related Services
Recommend this item
Bookmark
Usage statistics
Export to Endnote
Altmetrics Score
Google Scholar
Similar articles in Google Scholar
[Zhong, Chao]'s Articles
[Zhang, Fangyan]'s Articles
[Yao, Jia]'s Articles
Baidu academic
Similar articles in Baidu academic
[Zhong, Chao]'s Articles
[Zhang, Fangyan]'s Articles
[Yao, Jia]'s Articles
Bing Scholar
Similar articles in Bing Scholar
[Zhong, Chao]'s Articles
[Zhang, Fangyan]'s Articles
[Yao, Jia]'s Articles
Terms of Use
No data!
Social Bookmark/Share
No comment.
Items in the repository are protected by copyright, with all rights reserved, unless otherwise indicated.