Equation of State for Phospholipid Self-Assembly

被引:11
|
作者
Marsh, Derek [1 ,2 ]
机构
[1] Univ Southern Denmark, MEMPHYS, Odense, Denmark
[2] Max Planck Inst Biophys Chem, D-37077 Gottingen, Germany
关键词
CRITICAL MICELLE CONCENTRATION; MYELIN BASIC-PROTEIN; CALORIMETRIC DETERMINATION; HYDROPHOBIC INTERACTIONS; TEMPERATURE-DEPENDENCE; ENTROPY CONVERGENCE; HEAT-CAPACITY; SURFACE-AREA; CHAIN-LENGTH; THERMODYNAMICS;
D O I
10.1016/j.bpj.2015.11.012
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
Phospholipid self-assembly is the basis of biomembrane stability. The entropy of transfer from water to self-assembled micelles of lysophosphatidylcholines and diacyl phosphatidylcholines with different chain lengths converges to a common value at a temperature of 44 degrees C. The corresponding enthalpies of transfer converge at similar to-18 degrees C. An equation of state for the free energy of self-assembly formulated from this thermodynamic data depends on the heat capacity of transfer as the sole parameter needed to specify a particular lipid. For lipids lacking calorimetric data, measurement of the critical micelle concentration at a single temperature suffices to define an effective heat capacity according to the model. Agreement with the experimental temperature dependence of the critical micelle concentration is then good. The predictive powers should extend also to amphiphile partitioning and the kinetics of lipid-monomer transfer.
引用
收藏
页码:188 / 196
页数:9
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