Purification and structural characterization of a novel antibacterial peptide from Bellamya bengalensis: Activity against ampicillin and chloramphenicol resistant Staphylococcus epidermidis

被引:23
作者
Gauri, Samiran S. [2 ]
Mandal, Santi M. [1 ,2 ]
Pati, Bikas R. [2 ]
Dey, Satyahari [3 ]
机构
[1] Indian Inst Technol, Mass Spectrometry & Prote Lab, Cent Res Facil, Kharagpur 721302, W Bengal, India
[2] Vidyasagar Univ, Dept Microbiol, Midnapore 721102, WB, India
[3] Indian Inst Technol, Dept Biotechnol, Kharagpur 721302, W Bengal, India
关键词
Antimicrobial peptides; Antibiotic resistant; Mass spectrometry; Staphylococcus epidermidis; Bellamya bengalensis; ANTIMICROBIAL PEPTIDES; CATIONIC PEPTIDES; PROTEIN; INFECTIONS; SKIN; SUSCEPTIBILITY; DIVERSITY; MECHANISM; SEQUENCE;
D O I
10.1016/j.peptides.2011.01.014
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Increasing tendency of clinical bacterial strains resistant to conventional antibiotics has being a great challenge to the public's health. Antimicrobial peptides, a new class of antibiotics is known to have the activity against a wide range of bacteria resistant to conventional antibiotics. An antimicrobial peptide of 1676 Da was purified from Bellamya bengalensis, a fresh water snail, using ultrafiltration and reversed phase liquid chromatography. The effect of this peptide on Staphylococcus epidermidis resistant to ampicillin and chloramphenicol was investigated; the MIC and MBC values were 8 mu g/ml and 16 mu g/ml, respectively. Complete sequence of the peptide was determined by tandem mass spectrometry (MS/MS). Further, peptide net charge, hydrophobicity and molecular modeling were evaluated in silico for better understanding the probable mechanisms of action. The peptide showed the specificity to bacterial membranes. Hence, this reported peptide revealed a promising candidate to contribute in the development of therapeutic agent for Staphylococcal infections. (C) 2011 Elsevier Inc. All rights reserved.
引用
收藏
页码:691 / 696
页数:6
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