title: Are oblique orientated alpha-helices used by antimicrobial peptides for membrane invasion?
abstract: Oblique orientated alpha-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 alpha-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 alpha-helical structure.
authors.affiliation: Department of Forensic and Investigative Science, University of Central Lancashire, Preston, UK.
authors.forename: Sarah R
authors.initials: SR
authors.lastname: Dennison
authors.forename: Frederick
authors.initials: F
authors.lastname: Harris
authors.forename: David A
authors.initials: DA
authors.lastname: Phoenix
mesh_terms: D000595:Amino Acid Sequence; D029845:Amphibian Proteins / Q000737:chemistry; D000818:Animals; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry*; D002462:Cell Membrane / Q000737:chemistry* / Q000378:metabolism; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary
chemical_list: D029845:Amphibian Proteins; D023181:Antimicrobial Cationic Peptides; C121829:citropin 1.1 protein, Litoria