Lipid protrusions, membrane softness, and enzymatic activity

被引:28
|
作者
Hoyrup, P
Callisen, TH
Jensen, MO
Halperin, A
Mouritsen, OG
机构
[1] Tech Univ Denmark, Dept Chem, DK-2800 Lyngby, Denmark
[2] Tech Univ Denmark, Dept Phys, Quantum Prot Ctr, DK-2800 Lyngby, Denmark
[3] CEA, CENG, DRFMC SI3M, UMR 5819, F-38054 Grenoble 9, France
[4] Univ So Denmark, Dept Phys, MEMPHYS Ctr Biomembrane Phys, DK-5230 Odense M, Denmark
关键词
D O I
10.1039/b314146b
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
The activity of phospholipase A(2) on lipid bilayers displays a characteristic lag burst behavior that has previously been shown to reflect the physical properties of the substrate. It has remained unclear which underlying molecular mechanism is responsible for this phenomenon. We propose here that protrusions of single lipid molecules out of the bilayer plane could provide such a mechanism. The proposal is supported by a combination of atomic-scale molecular dynamics simulations, theory, and experiments that have been performed in order to investigate the relationship between on the one side lipid protrusion modes and mechanical softness of phospholipid bilayers and on the other side the activity of enzymes acting on lipid bilayers composed of different unsaturated lipids. Specifically, our experiments show a correlation between the bilayer bending rigidity and the apparent Arrhenius activation energy extracted from systematic lag-time versus temperature analyses.
引用
收藏
页码:1608 / 1615
页数:8
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