Literature DB >> 2605233

Temperature dependence of the vesicle-micelle transition of egg phosphatidylcholine and octyl glucoside.

M da Graça Miguel1, O Eidelman, M Ollivon, A Walter.   

Abstract

The temperature dependence of octyl glucoside micellization was determined and compared to the phase behavior of the octyl glucoside--egg phosphatidylcholine (PC) mixed system in excess water to help elucidate the process of vesicle formation from mixed surfactant-phospholipid micelles. The critical micelle concentration of octyl glucoside (OG) was determined from the sharp increase of ANS fluorescence at micellization in an NaCl buffer at temperatures ranging from 5 to 40 degrees C. The cmc decreased with increasing temperature from 31 mM at 5 degrees C to 16 mM at 40 degrees C. A similar but less steep temperature dependence is observed for the solubilization of egg PC vesicles by OG as monitored by the surfactant-dependent changes in (1) solution turbidity and (2) the resonance energy transfer between NBD-PE and Rho-PE incorporated in the vesicles. These assays identify two breakpoints, most likely the boundaries of the cylindrical micelle and spheroidal micelle coexistence region. The [OG]aq values at these two breakpoints have similar temperature dependencies. However, the cylindrical mixed micelles at the boundary have nearly identical OG:PC ratios over the temperature range studied, whereas the spheroidal mixed micelles have relatively more OG at the higher temperatures (OG:PC ratio increases from 2.92 to 3.72 between 5 and 35 degrees C). Estimation of the acyl volume to surface area ratio for the compositions observed suggests that this parameter remains constant over temperature. The spheroidal mixed micelles, but not the cylindrical PC-OG micelles, exhibit ideal mixing between the two components at all temperatures (5-35 degrees C). This temperature sensitivity may be utilized to improve the efficacy of membrane protein reconstitution.(ABSTRACT TRUNCATED AT 250 WORDS)

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Year:  1989        PMID: 2605233     DOI: 10.1021/bi00448a035

Source DB:  PubMed          Journal:  Biochemistry        ISSN: 0006-2960            Impact factor:   3.162


  14 in total

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3.  Partition coefficient of a surfactant between aggregates and solution: application to the micelle-vesicle transition of egg phosphatidylcholine and octyl beta-D-glucopyranoside.

Authors:  M Paternostre; O Meyer; C Grabielle-Madelmont; S Lesieur; M Ghanam; M Ollivon
Journal:  Biophys J       Date:  1995-12       Impact factor: 4.033

4.  Vesicle-micelle structural transition of phosphatidylcholine bilayers and Triton X-100.

Authors:  A De la Maza; J L Parra
Journal:  Biochem J       Date:  1994-11-01       Impact factor: 3.857

5.  Lipid bilayers in the gel phase become saturated by triton X-100 at lower surfactant concentrations than those in the fluid phase.

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6.  Self-assembling DNA-lipid particles for gene transfer.

Authors:  Y P Zhang; D L Reimer; G Zhang; P H Lee; M B Bally
Journal:  Pharm Res       Date:  1997-02       Impact factor: 4.200

7.  Amphiphilic, hydrophilic, or hydrophobic synthetic bacteriochlorins in biohybrid light-harvesting architectures: consideration of molecular designs.

Authors:  Jianbing Jiang; Kanumuri Ramesh Reddy; M Phani Pavan; Elisa Lubian; Michelle A Harris; Jieying Jiao; Dariusz M Niedzwiedzki; Christine Kirmaier; Pamela S Parkes-Loach; Paul A Loach; David F Bocian; Dewey Holten; Jonathan S Lindsey
Journal:  Photosynth Res       Date:  2014-07-05       Impact factor: 3.573

8.  Stages of the bilayer-micelle transition in the system phosphatidylcholine-C12E8 as studied by deuterium- and phosphorous-NMR, light scattering, and calorimetry.

Authors:  D Otten; L Löbbecke; K Beyer
Journal:  Biophys J       Date:  1995-02       Impact factor: 4.033

9.  Membrane solubilization with and reconstitution from surfactant solutions: a comparison of phosphatidylserine and phosphatidylcholine interactions with octyl glucoside.

Authors:  A Walter
Journal:  Mol Cell Biochem       Date:  1990-12-20       Impact factor: 3.396

10.  pH-dependent conformation, dynamics, and aromatic interaction of the gating tryptophan residue of the influenza M2 proton channel from solid-state NMR.

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Journal:  Biophys J       Date:  2013-04-16       Impact factor: 4.033

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