Structure and Biological Functions of β-Hairpin Antimicrobial Peptides

被引：48

作者：

Panteleev, P. V. ^{[1
]}

Bolosov, I. A. ^{[1
]}

Balandin, S. V. ^{[1
]}

Ovchinnikova, T. V. ^{[1
]}

机构：

[1] Russian Acad Sci, MM Shemyakin & Yu A Ovchinnikov Inst Bioorgan Ch, Moscow 117997, Russia

来源：

ACTA NATURAE | 2015年 / 7卷 / 01期

基金：

俄罗斯科学基金会;

关键词：

antimicrobial peptides; innate immunity; beta-hairpin structure; SPIDER ACANTHOSCURRIA-GOMESIANA; CRAB TACHYPLEUS-TRIDENTATUS; HERPES-SIMPLEX-VIRUS; AMINO-ACID-RESIDUES; THETA-DEFENSINS; ANTIBACTERIAL ACTIVITY; OLIGOMERIC STRUCTURE; DISULFIDE BRIDGES; LACTOFERRICIN-B; GENE-EXPRESSION;

D O I：

10.32607/20758251-2015-7-1-37-47

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 evolutionarily ancient factors of the innate immune system that serve as a crucial first line of defense for humans, animals, and plants against infection. This review focuses on the structural organization, biosynthesis, and biological functions of AMPs that possess a beta-hairpin spatial structure. Representatives of this class of AMPs are among the most active antibiotic molecules of animal origin. Due to their wide spectrum of activity and resistance to internal environmental factors, natural beta-hairpin AMP-based compounds might become the most promising drug candidates.

引用

页码：37 / 47

页数：11

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