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Parvin , Abraham and Sanil, George and K. Santhosh , Kumar (2014) Novel antibacterial peptides from the skin secretion of the Indian bicoloured frog Clinotarsus curtipes. Biochimie, 97. pp. 144-151. ISSN 1638-6183

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HPLC elution profile and MALDI TOF MS analysis of electro-stimulated skin secretion of the Indian Ranid frog Clinotarsus curtipes of the Western Ghats confirmed the presence of multiple peptides. Peptides eluted out of the C18 column at higher hydrophobic solvent region showed antibacterial activity against diverse bacterial strains, including the clinical isolates of V. cholerae and methicillin resistant Staphylococcus aureus (MRSA). Peptidomic analysis of the most potent chromatographic effluent fraction identified five novel peptide amides having sequence homology with brevinin family. These peptides are named as brevinin1CTcu1 (B1CTcu1) to brevinin1CTcu5 (B1CTcu5). Peptide B1CTcu1 is non-haemolytic while the others are haemolytic in nature but all elicited potential antibacterial activity. B1CTcu5 is a twenty-one residue peptide amide having proline hinge region in the middle and the typical C-terminal intramolecular disulfide-bridged hepta peptide domain (Rana box) that is present in most of the brevinin peptides. Analysis of their killing kinetics with E. coli and S. aureus and the ability to induce membrane depolarization proved that these are two independent events. These novel multifunctional peptides play an important role to protect C. curtipes from invading pathogenic microorganisms present in the environment.

Item Type: Article
Uncontrolled Keywords: Amphibian skin secretion; B1CTcu1–B1CTcu5; Clinotarsus curtipes; Host defense peptides (HDPs); Western Ghats
Subjects: Chemical Biology
Depositing User: Rgcb Library
Date Deposited: 16 Jan 2017 04:38
Last Modified: 16 Jan 2017 04:38
URI: http://rgcb.sciencecentral.in/id/eprint/158

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