Pore-forming bacteriocins: structural-functional relationships

被引：19
|
作者：
Vasilchenko, Alexey S. [1 ]
Valyshev, Alexander V. [2 ]
机构：
[1] Tyumen State Univ, Ul Volodarskogo 6, Tyumen 625003, Russia
[2] Russian Acad Sci, Inst Cellular & Intracellular Symbiosis, Ural Branch, Orenburg, Russia
来源：
ARCHIVES OF MICROBIOLOGY | 2019年 / 201卷 / 02期
关键词：
Bacteriocins; Antimicrobial peptides; Mode of action; Structural-functional relationships; 2-PEPTIDE BACTERIOCIN; CIRCULAR BACTERIOCIN; LIPID-II; ANTIMICROBIAL PEPTIDE; 3-DIMENSIONAL STRUCTURE; LANTIBIOTIC LACTICIN-3147; BACILLUS-SUBTILIS; PEDIOCIN PA-1; NISIN; AS-48;
D O I：
10.1007/s00203-018-1610-3
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
Peptides and proteins are important bioorganic compounds in nature, among which a special place is occupied by antimicrobial substances. There are more than 2000 different antimicrobial peptides (AMPs) produced by a variety of living organisms. Bacteriocins produced by bacteria are the minor group, whose chemical structures are most complicated among all AMPs. The review summarized the main points related to antimicrobial action of the bacteriocins including steps of peptide's interaction with bacterial membranes and details of membrane damaging. The membrane-disordered bacteriocins were described in accordance with structural-functional relationships.
引用
收藏
页码：147 / 154
页数：8
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