Antimicrobial Peptides: The Relationship of Their Structure and Antibacterial Activity

被引:0
|
作者
Dolezilkova, Ivana [1 ,2 ]
Mackova, Martina [1 ,2 ]
Macek, Tomas [1 ,2 ]
机构
[1] Vysoka Skola Chemickotechnol Praze, Ustav Biochem & Mikrobiol, Prague 16628 6, Czech Republic
[2] Spolecna Lab UOCHB AV CR & VSCHT Praha, Ustav Organ Chem& Biochem AV CR, Prague 16610 6, Czech Republic
来源
CHEMICKE LISTY | 2011年 / 105卷 / 05期
关键词
DODECYL-SULFATE MICELLES; GRAM-POSITIVE BACTERIA; TACHYPLESIN-I; ESCHERICHIA-COLI; LINEAR DERIVATIVES; MAGAININ PEPTIDES; INSECT PEPTIDE; BUFORIN II; MEMBRANE; INDOLICIDIN;
D O I
暂无
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Antimicrobial peptides (AMPs) are an important component of natural defence of most living organisms against invading pathogens. AMPs are mostly cationic and amphipathic peptides (mol. weight <10 kDa) of variable length, amino acid sequence and structure. In the past two decades several AMPs have been isolated from a wide variety of animals, both vertebrates and invertebrates, and plants as well as from bacteria and fungi. The peptides exhibit a broad-spectrum antimicrobial activity against a wide range of microorganisms including Gram-positive and Gram-negative bacteria, protozoa, yeasts, fungi and viruses. A few peptides are also cytotoxic to sperm and tumour cells. AMPs are classified by three-dimensional NMR structure analysis. To date, a number of AMPs have been chemically characterized. Structure-activity studies reveal two main requirements for antimicrobial activity - a positive charge and an induced amphipathic conformation. AMPs are excellent candidates for novel antimicrobial agents; a few peptides have undergone clinical trials.
引用
收藏
页码:346 / 355
页数:10
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