Interactions of Triton X-100 with sphingomyelin and phosphatidylcholine monolayers: Influence of the cholesterol content

被引:17
作者
Abi-Rizk, Georges [2 ,3 ]
Besson, Francoise [1 ,2 ,3 ]
机构
[1] Univ Lyon 1, CNRS, UMR5246, F-69622 Villeurbanne, France
[2] ICBMS, F-69622 Villeurbanne, France
[3] Univ Lyon, F-69622 Lyon, France
关键词
BAM; cholesterol; Langmuir film; phospholipid monolayer; Triton X-100;
D O I
10.1016/j.colsurfb.2008.06.002
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
The presence of microdomains, called lipid rafts, in biological membranes is usually explained by lateral segregation between specific lipids and proteins. These rafts present similarities with the membrane domains isolated by their non-ionic detergent-resistance at 4 degrees C. They are enriched in sphingomyelin and cholesterol as compared with the Outer leaflet of eukaryotic cell membranes. To understand the role played by the lipids enriched ill rafts in their resistance to solubilization by detergents, the interactions between these lipids and the non-ionic detergent Triton X-100 were Studied by using different lipid monolayers at the air-water interface. The influence of Triton X-100 on the Langmuir isotherms (i.e. surface pressure/area isotherms) of monolayers containing sphingomyelin and cholesterol at different mole ratios was analyzed and the results were compared with the influence of Triton X-100 on monolayers containing a phosphatidylcholine bearing a saturated and an unsaturated fatty acid (i.e. palmitoyloleylphosphatidylcholine) and cholesterol. This phosphatidylcholine was chosen since the phosphatidylcholines present in rafts isolated from bovine kidney could contain about 50% of saturated fatty acids. Triton X-100 induces an increase in the condensing effect observed as compared with ideal mixture of phospholipid/cholesterol. Triton X-100-induced changes in the morphology of the monolayers were visualized by Brewster angle microscopy, which confirmed the differences of behavior observed by analyzing the isotherms. (C) 2008 Elsevier B.V. All rights reserved.
引用
收藏
页码:163 / 167
页数:5
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