Antimicrobial properties of a lipid interactive alpha-helical peptide VP1 against Staphylococcus aureus bacteria.
Theoretical analysis indicates that peptide VP1 forms a membrane interactive amphiphilic alpha-helix with antibacterial properties. Fourier transform infra-red based analyses showed VP1 to be alpha-helical (45%) in the presence of vesicle mimics of membranes from Staphylococcus aureus and to induce increases in the fluidity of these vesicles, as indicated by a rise in wavenumber of circa 0.5 to 1.0 cm(-1). The peptide induced surface pressure increases of 5 mN m(-1) in monolayer mimics of S. aureus membranes confirm the formation of a membrane interactive alpha-helix. These interactions appeared to involve significant hydrophobic and electrostatic contributions as VP1 induced comparable surface pressure changes in anionic (5.5 mN m(-1)) and zwitterionic (4 mN m(-1)) lipid monolayers. It is suggested that whilst efficacy requires further sequence specific information, the peptides generic structure provides the basis for its broad antimicrobial activity.
Dennison
Sarah R
SR
Faculty of Science and Technology, University of Central Lancashire, Preston PR1 2HE, UK.
Morton
Leslie H G
LH
Harris
Frederick
F
Phoenix
David A
DA
D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000494:pharmacology*; D002462:Cell Membrane / Q000737:chemistry / Q000187:drug effects*; D008563:Membrane Lipids / Q000737:chemistry; D009842:Oligopeptides / Q000737:chemistry / Q000494:pharmacology*; D017433:Protein Structure, Secondary; D017550:Spectroscopy, Fourier Transform Infrared; D013211:Staphylococcus aureus / Q000187:drug effects* / Q000648:ultrastructure
D023181:Antimicrobial Cationic Peptides; D008563:Membrane Lipids; D009842:Oligopeptides; C523526:glycyl-threonyl-alanyl-methionyl-arginyl-isoleucyl-leucyl-glycyl-glycyl-valyl-isoleucine