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

► A novel antimicrobial peptide of 1676 Da was purified from venom of Bellamya bengalensis. ► Sequence of the peptide was determined by tandem mass spectrometry (MS/MS). ► The MIC and MBC values were 8 μg/ml and 16 μg/ml against Staphylococcus epidermidis resistant to ampicillin and chloramphenicol....

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Bibliographic Details
Published in:Peptides (New York, N.Y. : 1980) N.Y. : 1980), 2011-04, Vol.32 (4), p.691-696
Main Authors: Gauri, Samiran S., Mandal, Santi M., Pati, Bikas R., Dey, Satyahari
Format: Article
Language:English
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Summary:► A novel antimicrobial peptide of 1676 Da was purified from venom of Bellamya bengalensis. ► Sequence of the peptide was determined by tandem mass spectrometry (MS/MS). ► The MIC and MBC values were 8 μg/ml and 16 μg/ml against Staphylococcus epidermidis resistant to ampicillin and chloramphenicol. ► Peptide increased the staphylococcal membrane permeability. 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 μg/ml and 16 μg/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.
ISSN:0196-9781
1873-5169
DOI:10.1016/j.peptides.2011.01.014