Protein & Peptide Letters

Prof. Ben M. Dunn  
Department of Biochemistry and Molecular Biology
University of Florida
College of Medicine
P.O. Box 100245
Gainesville, FL
USA
Email: bdunn@ufl.edu

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Are Oblique Orientated α-Helices Used by Antimicrobial Peptides for Membrane Invasion?

Author(s): Sarah R. Dennison, Frederick Harris, David A. Phoenix.

Abstract:

Oblique orientated α-helices are highly specialised protein structural elements that penetrate membranes at a shallow angle and are used to promote membrane destabilisation by a number of protein classes. Here, the use of extended hydrophobic moment methodology shows that the amphibian extrudates, aurein 1.2 and citropin 1.1, may use oblique orientated α-helices in their antimicrobial action and that such use may be shared by other antimicrobial peptides. This appears to be the first systematic analysis of these peptides for the possession of oblique orientated a-helical structure.

Keywords: peptides, hydrophobicity, membrane destabilisation, haemolysis, non-bilayer lipid structures

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Article Details

VOLUME: 12
ISSUE: 1
Year: 2005
Page: [27 - 29]
Pages: 3
DOI: 10.2174/0929866053406039