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Membrane Lipid Composition and the Interaction of Pardaxin: The Role of Cholesterol

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Modulation by pardaxin of the phase transitions of dimyristoyl phosphatidylcholine, 1-stearoyl-2-oleoyl phosphatidylcholine or 1-stearoyl-2-oleoyl phosphatidylglycerol in the presence or absence of cholesterol was studied by differential scanning calorimetry. The transition enthalpy of each of the phospholipids was lowered by pardaxin and there was a small decrease in the transition temperature. Addition of cholesterol and pardaxin to dimyristoyl phosphatidylcholine resulted in a very marked lowering of the transition temperature. Although the peptide broadens the transition of the pure phospholipids, it sharpens the transition of mixtures of the phospholipids with cholesterol. This and the observation that pardaxin also causes the formation of crystallites of anhydrous cholesterol, suggest that the peptide promotes redistribution of cholesterol in the membrane.

Keywords: DSC; Pardaxin; cholesterol; membrane domains; phospholipid phase transitions

Document Type: Research Article


Affiliations: Department of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, ON Canada L8N 3Z5, Canada.

Publication date: January 1, 2006

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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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