Structure-function studies on the amphibian peptide brevinin 1E: translocating the cationic segment from the C-terminal end to a central position favors selective antibacterial activity

Kumari, V. K. ; Nagaraj, R. (2001) Structure-function studies on the amphibian peptide brevinin 1E: translocating the cationic segment from the C-terminal end to a central position favors selective antibacterial activity The Journal of Peptide Research, 58 (5). pp. 433-441. ISSN 1397-002X

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Official URL: http://onlinelibrary.wiley.com/doi/10.1034/j.1399-...

Related URL: http://dx.doi.org/10.1034/j.1399-3011.2001.00924.x

Abstract

Brevinin 1E, which has the sequence FLPLLAGLAANFLPKIFCKITRKC, is an antimicrobial peptide isolated from the skin secretions of the European frog Rana esculenta. Both the linear and the disulfide-bridged forms have relatively broad-spectrum antibacterial as well as hemolytic activities. The antibacterial and hemolytic activities and biophysical properties of synthetic peptides corresponding to brevinin 1E and its analog in which the segment CKITRKC has been transposed to a central location resulting in the sequence FLPLLAGLCKITRKCAANFLPKIF have been investigated. Our studies indicate that the analog peptide has antibacterial activity comparable with brevinin 1E, but with considerably reduced hemolytic activity. The linear variant of the analog has no hemolytic activity, unlike the linear form of brevinin 1E. The biological activities can be explained on the basis of relative affinities for anionic and zwitterionic lipids. A cluster of cationic amino acids flanked on one side by a hydrophobic stretch of amino acids and another side composed of apolar amino acids appears to favor preferential antibacterial activity.

Item Type:Article
Source:Copyright of this article belongs to John Wiley and Sons, Inc.
Keywords:Amphibian Skin Secretions; Antimicrobial Peptides; Hemolytic Activity; Lipid Interactions; Secondary Structure
ID Code:23935
Deposited On:01 Dec 2010 12:53
Last Modified:09 Jun 2011 08:18

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