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Journal Article

Equation of state for phospholipid self-assembly.

MPS-Authors
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Marsh,  D.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

External Resource
Fulltext (public)

2240820.pdf
(Publisher version), 909KB

Supplementary Material (public)

2240820_Suppl.ppt
(Supplementary material), 2MB

Citation

Marsh, D. (2016). Equation of state for phospholipid self-assembly. Biophysical Journal, 110(1), 188-196. doi:10.1016/j.bpj.2015.11.012.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0029-48C2-5
Abstract
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°C. The corresponding enthalpies of transfer converge at ∼−18°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.