## Abstract Two novel antimicrobial peptides with similarity to brevinin‐2 family are purified and characterized from the skin secretions of the frog, __Rana nigrovittata__. Their amino acid sequences were determined as GAFGNFLKGVAKKAGLKILSIAQCKLSGTC (__brevinin‐2‐RN1__) and GAFGNFLKGVAKKAGLKILSIAQ
Three novel antimicrobial peptides from the skin of the Indian bronzed frog Hylarana temporalis (Anura: Ranidae)
✍ Scribed by V. Reshmy; V. Preeji; A. Parvin; K. Santhoshkumar; S. George
- Publisher
- John Wiley and Sons
- Year
- 2011
- Tongue
- English
- Weight
- 328 KB
- Volume
- 17
- Category
- Article
- ISSN
- 1075-2617
- DOI
- 10.1002/psc.1363
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✦ Synopsis
Abstract
Amphibian skin secretion is considered as a rich source of bioactive peptides. The present work describes the successful identification of three novel peptides named brevinin‐1TEa, brevinin‐2TEa and brevinin‐2TEb present in the skin secretion of Indian bronzed frog Hylarana temporalis. The deduced open reading frame encoding the biosynthetic precursor of brevinin‐1TEa consisted of 70 amino acid residues and brevinin‐2TEa and brevinin‐2TEb consisted of 71 and 72 amino acids, respectively. All the three peptides showed higher antimicrobial activity against Gram‐negative than against Gram‐positive bacteria. On the basis of the antibacterial and haemolytic activity, brevinin‐2TEb is the most potent peptide reported in the present study. Further research on these peptides may provide potential clue towards newer drug development to combat various microbial diseases. Copyright © 2011 European Peptide Society and John Wiley & Sons, Ltd.
📜 SIMILAR VOLUMES
In this study, two novel antimicrobial peptides from the skin secretions of the marsh frog, __Rana ridibunda__, named temporin‐Ra and temporin‐Rb, were identified and purified using RP‐HPLC. Temporin‐Ra and temporin‐Rb are composed of 14 and 12 amino acids, respectively. Our results show that these