Evidence of entropic contribution to ''hydration'' forces between membranes .2. Temperature dependence of the ''hydration'' force: A small angle neutron scattering study
Evidence of entropic contribution to ''hydration'' forces between membranes .2. Temperature dependence of the ''hydration'' force: A small angle neutron scattering study
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DOI:
10.1016/s0022-2860(96)09276-9
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发表时间:
1996-09-30
影响因子:
3.8
通讯作者:
Teixeira, J
中科院分区:
文献类型:
--
作者:
Gordeliy, VI;Cherezov, VG;Teixeira, J
The temperature dependence of structural parameters of 1,2-dimiristoyl-sn-glycero-phosphatidylcholine (DMPC) and 1,2-dipalmitoyl-sn-glycero-phosphatidylcholine (DPPC) membranes in D2O (1% w/w of lipid) has been studied via neutron small-angle scattering.A new approach was used to determine the intermembrane distance d(w). The repeat distance d was determined from the position of diffraction peaks from multilamellar membranes in solution. The thickness of membranes d(L) was calculated from small-angle scattering with single vesicles. The intermembrane distance d, was determined as the difference between d and d(L).Repeat and intermembrane distances increase considerably with temperature increase at T > 65 degrees C. However, the lipid bilayer thickness decreases continuously with the increase of temperature. The integral intensities of the diffraction peaks decrease considerably.It is shown here that the temperature dependence of the intermembrane distance can be explained by the increase of entropic forces due to an increase of protrusion-like thermal fluctuations of the membrane surface and membrane undulations. The membrane undulations increase due to the decrease of membrane bending rigidity. Considerable changes in the bending rigidity with temperature cannot be explained only by the reduction of the bilayer thickness. The increase of protrusion amplitude with temperature increase results in a dramatic decrease of the bending rigidity.