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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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Published in: | Peptides (New York, N.Y. : 1980) N.Y. : 1980), 2011-04, Vol.32 (4), p.691-696 |
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Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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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. |
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ISSN: | 0196-9781 1873-5169 |
DOI: | 10.1016/j.peptides.2011.01.014 |