A differential scanning calorimetry study of the effects and interactions of antimicrobial peptide LS3 on phosphatidylethanolamine bilayers.
Differential Scanning Calorimetry studies of a synthetic peptide revealed the peptide decreased the temperature of the lamellar-hexagonal phase transition of cis-trans mixtures of phosphatidylethanolamine. The transition enthalpy varied significantly with lipid composition. The findings are discussed with reference to peptide saturation on the bilayer surface, bilayer thinning and peptide orientation.
Sa'adedin
Farid
F
Royal (Dick) School of Veterinary Studies, The University of Edinburgh, Easter Bush Veterinary Centre, Roslin, Midlothian, EH25 9RG, UK. s0094154@sms.ed.ac.uk
Bradshaw
Jeremy P
JP
D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000378:metabolism; D002152:Calorimetry, Differential Scanning; D036341:Intercellular Signaling Peptides and Proteins; D008051:Lipid Bilayers / Q000737:chemistry* / Q000378:metabolism; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D010714:Phosphatidylethanolamines / Q000737:chemistry* / Q000378:metabolism; D013816:Thermodynamics; D044366:Transition Temperature
D023181:Antimicrobial Cationic Peptides; D036341:Intercellular Signaling Peptides and Proteins; C538946:LS3 peptide; D008051:Lipid Bilayers; D010455:Peptides; D010714:Phosphatidylethanolamines; C483858:phosphatidylethanolamine