The electrostatics of lipid surfaces

被引:146
作者
Langner, M [1 ]
Kubica, K [1 ]
机构
[1] Univ Agr, Dept Phys & Biophys, PL-50375 Wroclaw, Poland
关键词
charged lipids; membrane electrostatics; molecular recognition; surface specificity;
D O I
10.1016/S0009-3084(99)00052-3
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
Charged lipids constitute a substantial fraction of all membrane lipids. Their charges vary in quantity and distribution within their headgroup regions. In long range interactions, their charges' value and electrostatic potential in the vicinity of the membrane surface can be approximated by the Guy-Chapman theory. This theory treats the interface as a charged structureless plain surrounded by uniform environments. However, if one considers intermolecular interactions, such assumptions need to be revised. The interface is in reality a thick region containing the residual charges of lipid headgroups. Their arrangement depends on the type of lipid present in the membrane. The variety of lipids and their biological functions suggests that charge distribution determines the extent and type of interaction with surface associated molecules. Numerous examples show that protein behavior at the lipid bilayer surface is determined by the type of lipid present, indicating protein specificity towards certain surface locations and local properties (determined by lipid composition) of a particular type. Such specificity is achieved by a combination-of electrostatic, hydrophobic and enthropic effects. Comparing lipid biological activity, it can be stated that residual charge distribution is one of the factors of intermolecular recognition leading to the specific interaction of lipid molecules and selected proteins in various processes, particularly those involved with signal transduction pathways. Such specificity enables a variety of processes occurring simultaneously on the same membrane surface to function without cross-reaction interference. (C) 1999 Published by Elsevier Science Ireland Ltd. All rights reserved.
引用
收藏
页码:3 / 35
页数:33
相关论文
共 296 条
[1]   CELL-SURFACE RECEPTORS FOR EXTRACELLULAR-MATRIX COMPONENTS [J].
AKIYAMA, SK ;
NAGATA, K ;
YAMADA, KM .
BIOCHIMICA ET BIOPHYSICA ACTA, 1990, 1031 (01) :91-110
[2]   CONFORMATIONAL-ANALYSIS OF THE POLAR HEAD GROUP IN PHOSPHATIDYLCHOLINE BILAYERS - A STRUCTURAL-CHANGE INDUCED BY CATIONS [J].
AKUTSU, H ;
NAGAMORI, T .
BIOCHEMISTRY, 1991, 30 (18) :4510-4516
[3]   CA-2+ BINDING TO PHOSPHATIDYLCHOLINE BILAYERS AS STUDIED BY DEUTERIUM MAGNETIC-RESONANCE - EVIDENCE FOR THE FORMATION OF A CA-2+ COMPLEX WITH 2 PHOSPHOLIPIDMOLECULES [J].
ALTENBACH, C ;
SEELIG, J .
BIOCHEMISTRY, 1984, 23 (17) :3913-3920
[4]   MEMBRANE-PROTEIN TOPOLOGY - EFFECTS OF DELTA-MU(H)+ ON THE TRANSLOCATION OF CHARGED RESIDUES EXPLAIN THE POSITIVE INSIDE RULE [J].
ANDERSSON, H ;
VONHEIJNE, G .
EMBO JOURNAL, 1994, 13 (10) :2267-2272
[5]   DETECTION OF PROTEIN MEDIATED GLYCOSPHINGOLIPID CLUSTERING BY THE USE OF RESONANCE ENERGY-TRANSFER BETWEEN FLUORESCENT LABELED LIPIDS - A METHOD ESTABLISHED BY APPLYING THE SYSTEM GANGLIOSIDE GM1 AND CHOLERA TOXIN-B SUBUNIT [J].
ANTES, P ;
SCHWARZMANN, G ;
SANDHOFF, K .
CHEMISTRY AND PHYSICS OF LIPIDS, 1992, 62 (03) :269-280
[6]   Coupling of proton source and sink via H+-migration along the membrane surface as revealed by double patch-clamp experiments [J].
Antonenko, YN ;
Pohl, P .
FEBS LETTERS, 1998, 429 (02) :197-200
[7]   Permeation of ammonia across bilayer lipid membranes studied by ammonium ion selective microelectrodes [J].
Antonenko, YN ;
Pohl, P ;
Denisov, GA .
BIOPHYSICAL JOURNAL, 1997, 72 (05) :2187-2195
[8]   WEAK ACID TRANSPORT ACROSS BILAYER-LIPID MEMBRANE IN THE PRESENCE OF BUFFERS - THEORETICAL AND EXPERIMENTAL PH PROFILES IN THE UNSTIRRED LAYERS [J].
ANTONENKO, YN ;
DENISOV, GA ;
POHL, P .
BIOPHYSICAL JOURNAL, 1993, 64 (06) :1701-1710
[9]   Visualization of the reaction layer in the immediate membrane vicinity [J].
Antonenko, YN ;
Pohl, P ;
Rosenfeld, E .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1996, 333 (01) :225-232
[10]   Kinetics of interaction of the myristoylated alanine-rich C kinase substrate, membranes, and calmodulin [J].
Arbuzova, A ;
Wang, JY ;
Murray, D ;
Jacob, J ;
Cafiso, DS ;
McLaughlin, S .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (43) :27167-27177