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A Differential Scanning Calorimetry Study of the Effects and Interactions of Antimicrobial Peptide LS3 on Phosphatidylethanolamine Bilayers

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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: (DSC); (LSSLLSL)3; (MLVs); Antimicrobial; Antimicrobial peptide; DOPE; DPOPE; DSC; EDTA; LS3; PE bilayers; TH; amphipathic; amphipathic helix; bilayer; crystallography; phase; phase transition; phosphatidylethanolamine

Document Type: Research Article

Publication date: November 1, 2010

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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