کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
613174 880717 2006 10 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Phase behavior and the partitioning of caveolin-1 scaffolding domain peptides in model lipid bilayers
موضوعات مرتبط
مهندسی و علوم پایه مهندسی شیمی شیمی کلوئیدی و سطحی
پیش نمایش صفحه اول مقاله
Phase behavior and the partitioning of caveolin-1 scaffolding domain peptides in model lipid bilayers
چکیده انگلیسی

The membrane binding and model lipid raft interaction of synthetic peptides derived from the caveolin scaffolding domain (CSD) of the protein caveolin-1 have been investigated. CSD peptides bind preferentially to liquid-disordered domains in model lipid bilayers composed of cholesterol and an equimolar ratio of dioleoylphosphatidylcholine (DOPC) and brain sphingomyelin. Three caveolin-1 peptides were studied: the scaffolding domain (residues 83–101), a water-insoluble construct containing residues 89–101, and a water-soluble construct containing residues 89–101. Confocal and fluorescence microscopy investigation shows that the caveolin-1 peptides bind to the more fluid cholesterol-poor phase. The binding of the water-soluble peptide to lipid bilayers was measured using fluorescence correlation spectroscopy (FCS). We measured molar partition coefficients of 104 M−1 between the soluble peptide and phase-separated lipid bilayers and 103 M−1 between the soluble peptide and bilayers with a single liquid phase. Partial phase diagrams for our phase-separating lipid mixture with added caveolin-1 peptides were measured using fluorescence microscopy. The water-soluble peptide did not change the phase morphology or the miscibility transition in giant unilamellar vesicles (GUVs); however, the water-insoluble and full-length CSD peptides lowered the liquid–liquid melting temperature.

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ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Colloid and Interface Science - Volume 304, Issue 1, 1 December 2006, Pages 67–76
نویسندگان
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