Antibacterial activity of lactophoricin, a synthetic 23-residues peptide derived from the sequence of bovine milk component-3 of proteose peptone

被引:55
作者
Campagna, S
Mathot, AG
Fleury, Y
Girardet, JM
Gaillard, JL
机构
[1] Univ Nancy 1, INRA, UC 885, Lab Biosci Aliment, F-54506 Vandoeuvre Les Nancy, France
[2] Lab Univ Microbiol Appl Quimper, EA 2651, F-29334 Quimper, France
关键词
bovine milk; component-3 3 of proteose peptone; antimicrobial activity; amphipathic peptide;
D O I
10.3168/jds.S0022-0302(04)73316-0
中图分类号
S8 [畜牧、 动物医学、狩猎、蚕、蜂];
学科分类号
0905 [畜牧学];
摘要
A synthetic peptide of 23 residues corresponding to the carboxyterminal 113 to 135 region of component-3 of proteose peptone (PP3) has been investigated with regard to its antibacterial properties. This cationic amphipathic peptide that we refer to as lactophoricin, displayed a growth-inhibitory activity against both gram-positive and gram-negative bacteria. For most of the strains tested, bacterial growth was observed in the presence of lactophoricin except for Streptococcus thermophilus. In that case, lactophoricin exhibited a minimum inhibitory concentration of 10 muM and a minimum lethal concentration of 20 muM. No hemolysis of human red blood cells was detected for peptide concentrations between 2 to 200 muM, indicating that lactophoricin would be noncytotoxic when used in this concentration range.
引用
收藏
页码:1621 / 1626
页数:6
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