Lipid membrane domain formation and alamethicin aggregation studied by calorimetry, sound velocity measurements, and atomic force microscopy

被引:15
|
作者
Oliynyk, Vitaliy [1 ,2 ]
Jaeger, Markus [1 ]
Heimburg, Thomas [2 ]
Buckin, Vitaly [3 ]
Kaatze, Udo [1 ]
机构
[1] Univ Gottingen, Complex Fluids Grp, Drittes Phys Inst, D-37077 Gottingen, Germany
[2] Univ Copenhagen, Membrane Biophys Grp, Niels Bohr Inst, DK-2100 Copenhagen, Denmark
[3] Univ Coll Dublin, Sch Chem & Chem Biol, Dublin 4, Ireland
关键词
lipid membranes; alamethicin; peptide pores; atomic force microscopy; sound velocity; differential scanning calorimetry;
D O I
10.1016/j.bpc.2008.02.004
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
An experimental study of phosphocholine membranes made from one lipid, from mixtures of DPPC and DLPC, and also from lipids and small amounts of alamethicin is presented. We used atomic force microscopy to investigate the spatial organization and structure of lipid domains and also of the defects induced by the peptide. Alamethicin was found to alter the state of lipids in the gel state in a way that domains of fluid lipids are formed close to the defects. Differential calorimetry revealed phase characteristics of the lipid mixtures and the effect of small amounts of alamethicin on the phase behavior. It was also shown that the sound velocity profiles of the membranes suspensions can be well calculated from the heat capacity traces of the samples. This result confirms the correlation between the mechanical properties and the specific heat of membrane systems. (c) 2008 Elsevier B.V. All rights reserved.
引用
收藏
页码:168 / 177
页数:10
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