Are Oblique Orientated α-Helices Used by Antimicrobial Peptides for Membrane Invasion?
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: haemolysis; hydrophobicity; membrane destabilisation; non-bilayer lipid structures; peptides
Document Type: Review Article
Affiliations: Deans Office, Faculty of Science, University of Central Lancashire, Preston, PR1 2HE, UK.
Publication date: 01 January 2005
- Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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