Abstract
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.
Keywords: Antimicrobial peptide, amphipathic helix, DSC, LS3, phosphatidylethanolamine, phase transition, Antimicrobial, amphipathic, phase, (LSSLLSL)3, bilayer, (DSC), crystallography, DOPE, (MLVs), EDTA, TH, PE bilayers, DPOPE
Protein & Peptide Letters
Title: A Differential Scanning Calorimetry Study of the Effects and Interactions of Antimicrobial Peptide LS3 on Phosphatidylethanolamine Bilayers
Volume: 17 Issue: 11
Author(s): Farid Sa'adedin and Jeremy P. Bradshaw
Affiliation:
Keywords: Antimicrobial peptide, amphipathic helix, DSC, LS3, phosphatidylethanolamine, phase transition, Antimicrobial, amphipathic, phase, (LSSLLSL)3, bilayer, (DSC), crystallography, DOPE, (MLVs), EDTA, TH, PE bilayers, DPOPE
Abstract: 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.
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Cite this article as:
Sa'adedin Farid and P. Bradshaw Jeremy, A Differential Scanning Calorimetry Study of the Effects and Interactions of Antimicrobial Peptide LS3 on Phosphatidylethanolamine Bilayers, Protein & Peptide Letters 2010; 17 (11) . https://dx.doi.org/10.2174/0929866511009011345
DOI https://dx.doi.org/10.2174/0929866511009011345 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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