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Purification and structural characterization of a novel antibacterial peptide from Bellamya bengalensis: Activity against ampicillin and chloramphenicol resistant Staphylococcus epidermidis
- Source :
- Peptides. 32:691-696
- Publication Year :
- 2011
- Publisher :
- Elsevier BV, 2011.
-
Abstract
- 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.
- Subjects :
- Physiology
medicine.drug_class
Snails
Antibiotics
Antimicrobial peptides
Peptide
Microbial Sensitivity Tests
Biochemistry
Microbiology
Cellular and Molecular Neuroscience
Endocrinology
Tandem Mass Spectrometry
Staphylococcus epidermidis
Ampicillin
medicine
Animals
Antibacterial agent
chemistry.chemical_classification
biology
Chemistry
Chloramphenicol
Drug Resistance, Microbial
Flow Cytometry
Antimicrobial
biology.organism_classification
Anti-Bacterial Agents
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Microscopy, Electron, Scanning
Peptides
Chromatography, Liquid
medicine.drug
Subjects
Details
- ISSN :
- 01969781
- Volume :
- 32
- Database :
- OpenAIRE
- Journal :
- Peptides
- Accession number :
- edsair.doi.dedup.....43ba1afa1fa7d5c13294f667a8698edf
- Full Text :
- https://doi.org/10.1016/j.peptides.2011.01.014