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Relationship between peptide structure and antimicrobial activity as studied by de novo designed peptides
Liang, Dehai1,2; Sun, Jianbo1,2; Xia, Yuqiong3; Li, Dong4; Du, Quan4
关键词Antimicrobial Peptide Membrane Leakage Fusion Aggregation
刊名BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
2014-12-01
DOI10.1016/j.bbamem.2014.08.018
1838期:12页:2985-2993
收录类别SCI
文章类型Article
WOS标题词Science & Technology
类目[WOS]Biochemistry & Molecular Biology ; Biophysics
研究领域[WOS]Biochemistry & Molecular Biology ; Biophysics
关键词[WOS]MEMBRANE-FUSION ; PHOSPHATIDYLETHANOLAMINE LIPOSOMES ; ESCHERICHIA-COLI ; MAGAININ 2 ; MECHANISM ; VESICLES ; BACTERIA ; LENGTH ; PHASE ; DESTABILIZATION
英文摘要

As fundamental components in innate immunity, antimicrobial peptides (AMPS) hold great potentials in the treatment of persistent infections involving slow-growing or dormant bacteria in which, selective inhibition of prokaryotic bacteria in the context of eukaryotic cells is not only an essential requirement, but also a critical challenge in the development of antimicrobial peptides. To identify the sequence and structural properties critical for antimicrobial activity, a series of peptides varying in sequence, length, hydrophobicity/charge ratio, and secondary structure, were designed and synthesized. Their antimicrobial activities were then tested using Escherichia coli and HEK293 cells, together with several index activities against model membrane, including liposome leakage, fusion, and aggregation. While no evident correlation between the antimicrobial activity and the property of the peptides was observed, common activities against model membrane were nevertheless identified for the active antimicrobial peptides: mediating efficient membrane leakage, negligible membrane fusion and liposome aggregation. Therefore, in addition to identifying one highly active antimicrobial peptide, our study further sheds light on the design principle for these molecules. (C) 2014 Elsevier B.V. All rights reserved.

语种英语
WOS记录号WOS:000343847200002
引用统计
被引频次:11[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.bjmu.edu.cn/handle/400002259/50245
专题北京大学第一临床医学院_病理科
北京大学药学院
作者单位1.Peking Univ, Coll Chem & Mol Engn, Minist Educ, Beijing 100871, Peoples R China
2.Peking Univ, Coll Chem & Mol Engn, Key Lab Polymer Chem & Phys, Minist Educ, Beijing 100871, Peoples R China
3.Xidian Univ, Sch Life Sci & Technol, Xian 710126, Shaanxi, Peoples R China
4.Peking Univ, Sch Pharmaceut Sci, State Key Lab Nat & Biomimet Drugs, Beijing 100871, Peoples R China
推荐引用方式
GB/T 7714
Liang, Dehai,Sun, Jianbo,Xia, Yuqiong,et al. Relationship between peptide structure and antimicrobial activity as studied by de novo designed peptides[J]. BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES,2014,1838(12):2985-2993.
APA Liang, Dehai,Sun, Jianbo,Xia, Yuqiong,Li, Dong,&Du, Quan.(2014).Relationship between peptide structure and antimicrobial activity as studied by de novo designed peptides.BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES,1838(12),2985-2993.
MLA Liang, Dehai,et al."Relationship between peptide structure and antimicrobial activity as studied by de novo designed peptides".BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES 1838.12(2014):2985-2993.
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