Role of peptide self-assembly in antimicrobial peptides

被引:96
|
作者
Tian, Xibo [1 ]
Sun, Fude [1 ]
Zhou, Xi-Rui [1 ]
Luo, Shi-Zhong [1 ]
Chen, Long [1 ]
机构
[1] Beijing Univ Chem Technol, Coll Life Sci & Technol, Beijing Key Lab Bioproc, Beijing 100029, Peoples R China
基金
中国国家自然科学基金;
关键词
antimicrobial peptides; peptide self-assembly; cell selectivity; stability; drug delivery; STATE NMR-SPECTROSCOPY; MOLECULAR-DYNAMICS; CATIONIC PEPTIDES; CELL SELECTIVITY; DESIGNED PEPTIDE; LYTIC PEPTIDE; MEMBRANE; ANTIBACTERIAL; HYDROGELATION; PH;
D O I
10.1002/psc.2788
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Antimicrobial peptides (AMPs) are considered as potential antibiotic substitutes because of their potent activities. Previous studies mainly focused on the effects of peptide charges and secondary structures, but the self-assembly of AMPs was neglected. As more and more researchers notice the roles of peptide self-assembly in AMPs, it has been considered as another important property. In this review, we will discuss the influences of peptide self-assembly on the activity and mode of action, and some specific features it introduces to the AMPs, such as particular responsiveness, improved cell selectivity and stability and sustained release. In addition, some methods to design self-assembling AMPs are primarily discussed. With further understanding about the self-assembling regularity, design of particular self-assembling AMPs will be very helpful for their applications, especially in the fields of drug delivery and biomedical engineering. Copyright (c) 2015 European Peptide Society and John Wiley & Sons, Ltd.
引用
收藏
页码:530 / 539
页数:10
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