title: Amphiphilic alpha-helical antimicrobial peptides and their structure/function relationships.
abstract: To facilitate microbial membrane invasion, amphiphilic alpha-helical antimicrobial peptides (alpha-AMPs) show a spatial segregation of hydrophobic and hydrophilic residues about the alpha-helical long axis. Here we discuss potential mechanisms by which these peptides are able to disrupt membrane structure and the structural characteristics, which are required for function.
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: James
authors.initials: J
authors.lastname: Wallace
authors.forename: Frederick
authors.initials: F
authors.lastname: Harris
authors.forename: David A
authors.initials: DA
authors.lastname: Phoenix
mesh_terms: D000596:Amino Acids / Q000737:chemistry; D000818:Animals; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry* / Q000378:metabolism; D002462:Cell Membrane / Q000737:chemistry; D008958:Models, Molecular; D013329:Structure-Activity Relationship; D013501:Surface-Active Agents / Q000737:chemistry
chemical_list: D000596:Amino Acids; D023181:Antimicrobial Cationic Peptides; D013501:Surface-Active Agents