RYH: A minimal peptidic sequence obtained from beta-chain hemoglobin exhibiting an antimicrobial activity

被引：40

作者：

Catiau, Lucie ^{[1
]}

Traisnel, Johnatan ^{[1
]}

Chihib, Nour-Eddine ^{[1
]}

Le Flem, Guillaume ^{[1
]}

Blanpain, Annick ^{[2
]}

Melnyk, Oleg ^{[2
]}

Guillochon, Didier ^{[1
]}

Nedjar-Arroume, Naima ^{[1
]}

机构：

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

[2] Inst Biol Lille, UMR CNRS 8161, F-59021 Lille, France

来源：

PEPTIDES | 2011年 / 32卷 / 07期

关键词：

Hemoglobin; Antimicrobial; MIC; Bacteriostatic effect; Liposome; Minimal sequence; BOVINE HEMOGLOBIN; ANTIBACTERIAL ACTIVITY; IDENTIFICATION; HYDROLYSIS; NEOKYOTORPHIN; APPEARANCE; FRAGMENT; DOMAIN; ACID;

D O I：

10.1016/j.peptides.2011.05.021

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：

Bovine hemoglobin is an animal protein described as source of bioactive peptides. Enzymatic hydrolysis of this protein results into some peptides exhibiting antimicrobial activity against Gram-positive and Gram-negative bacteria. In this study, a family of peptides from the beta chain (beta-114-145 derived peptides) obtained by peptic hydrolysis of bovine hemoglobin, was purified by reverse-phase HPLC and characterized by different analytical techniques (mass spectrometry, circular dichroism). The minimum inhibitory concentration was determined to show the antimicrobial activity of these peptides. Four bacterial strains were used: two Gram-negative (Escherichia coli and Salmonella Enteritidis) and two Gram-positive strains (Listeria innocua and Micrococcus luteus). The effect of these peptides on artificial membrane was also measured. Our findings showed that the peptide beta 114-145 and its peptic derivatives contain the RYH sequence. The most antimicrobial peptide is the RYH peptide which was the shortest one. (C) 2011 Elsevier Inc. All rights reserved.

引用

页码：1463 / 1468

页数：6

共 25 条

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