Biological activities and structural properties of the atypical bacteriocins mesenterocin 52B and leucocin B-TA33a

被引：15

作者：

Corbier, C

Krier, F

Mulliert, G

Vitoux, B

Revol-Junelles, AM

机构：

[1] Ecole Natl Super Agron & Ind Alimentaires, Lab Bioprocedes Agroalimentaires, Inst Natl Polytech Lorraine, F-54505 Vandoeuvre Les Nancy, France

[2] Univ Nancy 1, Grp Biocristallog, UPRESA CNRS 7036, Lab Cristallog & Modelisat Mat Mineraux & Biol, F-54506 Vandoeuvre Les Nancy, France

来源：

APPLIED AND ENVIRONMENTAL MICROBIOLOGY | 2001年 / 67卷 / 04期

关键词：

D O I：

10.1128/AEM.67.4.1418-1422.2001

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

The antibacterial spectra and modes of action of synthetic peptides corresponding to mesenterocin 52B and leucocin B-TA33a greatly differ despite their high sequence homology. Circular dichroism experiments establish the capacity of each of these two peptides to partly fold into an amphiphilic helix that might be crucial for their adsorption at lipophilic-hydrophilic interfaces.

引用

页码：1418 / 1422

页数：5

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