Minimal antimicrobial peptidic sequence from hemoglobin alpha-chain: KYR

被引：75

作者：

Catiau, Lucie ^{[1
]}

Traisnel, Johnatan ^{[1
]}

Delval-Dubois, Veronique ^{[1
]}

Chihib, Nour-Eddine ^{[1
]}

Guillochon, Didier ^{[1
]}

Nedjar-Arroume, Naima ^{[1
]}

机构：

[1] Lab ProBioGEM, F-59655 Villeneuve Dascq, France

来源：

PEPTIDES | 2011年 / 32卷 / 04期

关键词：

Hemoglobin; Antimicrobial; MIC; Liposome; Minimal sequence; PHOTODIODE-ARRAY DETECTION; BOVINE HEMOGLOBIN; OPIOID-PEPTIDES; ANTIBACTERIAL ACTIVITY; INHIBITORY PEPTIDES; BIOACTIVE PEPTIDES; PROTEIN; HYDROLYSIS; APPEARANCE; HEMORPHINS;

D O I：

10.1016/j.peptides.2010.12.016

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

Hemoglobin is an animal protein described as a source of biologically active peptides. Peptic digestion of bovine hemoglobin alpha-chain allowed obtaining peptide fractions with antimicrobial activity. These peptides were purified by reverse-phase High-Performance Liquid Chromatography (HPLC) and characterized by mass spectrometry. The minimal inhibitory concentration and mode of action of these peptides were studied against five bacterial strains including Escherichia coli and Salmonella enteritidis as Gram-negative bacteria and Listeria innocua, Micrococcus luteus and Staphylococcus aureus as Gram-positive bacteria. The action aforementioned peptides were studied on artificial membranes as well. The most active peptides resulted to be the short ones. Consequently, the minimal peptidic sequence necessary for the antibacterial activity was clearly determined: KYR. (C) 2011 Elsevier Inc. All rights reserved.

引用

页码：633 / 638

页数：6

共 28 条

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DETERMINATION OF THE DEGREE OF HYDROLYSIS OF FOOD PROTEIN HYDROLYSATES BY TRINITROBENZENESULFONIC ACID [J].