Simulation studies of protein-induced bilayer deformations, and lipid-induced protein tilting, on a mesoscopic model for lipid bilayers with embedded proteins

被引:207
作者
Venturoli, M
Smit, B
Sperotto, MM [1 ]
机构
[1] Tech Univ Denmark, Bioctr, Kgs Lyngby, Denmark
[2] Univ Amsterdam, Dept Chem Engn, NL-1018 WV Amsterdam, Netherlands
[3] UCL, Dept Chem, London, England
关键词
D O I
10.1529/biophysj.104.050849
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
Biological membranes are complex and highly cooperative structures. To relate biomembrane structure to their biological function it is often necessary to consider simpler systems. Lipid bilayers composed of one or two lipid species, and with embedded proteins, provide a model system for biological membranes. Here we present a mesoscopic model for lipid bilayers with embedded proteins, which we have studied with the help of the dissipative particle dynamics simulation technique. Because hydrophobic matching is believed to be one of the main physical mechanisms regulating lipid-protein interactions in membranes, we considered proteins of different hydrophobic length ( as well as different sizes). We studied the cooperative behavior of the lipid-protein system at mesoscopic time-and lengthscales. In particular, we correlated in a systematic way the protein-induced bilayer perturbation, and the lipid-induced protein tilt, with the hydrophobic mismatch ( positive and negative) between the protein hydrophobic length and the pure lipid bilayer hydrophobic thickness. The protein-induced bilayer perturbation was quantified in terms of a coherence length, xi(P), of the lipid bilayer hydrophobic thickness pro. le around the protein. The dependence on temperature of xi(P), and the protein tilt-angle, were studied above the main-transition temperature of the pure system, i.e., in the fluid phase. We found that xi(P) depends on mismatch, i.e., the higher the mismatch is, the longer xi(P) becomes, at least for positive values of mismatch; a dependence on the protein size appears as well. In the case of large model proteins experiencing extreme mismatch conditions, in the region next to the so-called lipid annulus, there appears an undershooting ( or overshooting) region where the bilayer hydrophobic thickness is locally lower ( or higher) than in the unperturbed bilayer, depending on whether the protein hydrophobic length is longer ( or shorter) than the pure lipid bilayer hydrophobic thickness. Proteins may tilt when embedded in a too-thin bilayer. Our simulation data suggest that, when the embedded protein has a small size, the main mechanism to compensate for a large hydrophobic mismatch is the tilt, whereas large proteins react to negative mismatch by causing an increase of the hydrophobic thickness of the nearby bilayer. Furthermore, for the case of small, peptidelike proteins, we found the same type of functional dependence of the protein tilt-angle on mismatch, as was recently detected by fluorescence spectroscopy measurements.
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页码:1778 / 1798
页数:21
相关论文
共 120 条
[1]   STRUCTURAL ORGANIZATION OF THE PENTAMERIC TRANSMEMBRANE ALPHA-HELICES OF PHOSPHOLAMBAN, A CARDIAC ION-CHANNEL [J].
ARKIN, IT ;
ADAMS, PD ;
MACKENZIE, KR ;
LEMMON, MA ;
BRUNGER, AT ;
ENGELMAN, DM .
EMBO JOURNAL, 1994, 13 (20) :4757-4764
[2]  
Bechinger B, 1997, PROTEINS, V27, P481, DOI 10.1002/(SICI)1097-0134(199704)27:4<481::AID-PROT2>3.3.CO
[3]  
2-6
[4]   The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy [J].
Bechinger, B .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 1999, 1462 (1-2) :157-183
[5]   Structure and dynamics of an amphiphilic peptide in a lipid bilayer: A molecular dynamics study [J].
Belohorcova, K ;
Davis, JH ;
Woolf, TB ;
Roux, B .
BIOPHYSICAL JOURNAL, 1997, 73 (06) :3039-3055
[6]   Molecular dynamics and 2H-NMR study of the influence of an amphiphilic peptide on membrane order and dynamics [J].
Belohorcová, K ;
Qian, J ;
Davis, JH .
BIOPHYSICAL JOURNAL, 2000, 79 (06) :3201-3216
[7]   Domains and rafts in lipid membranes [J].
Binder, WH ;
Barragan, V ;
Menger, FM .
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 2003, 42 (47) :5802-5827
[8]   Interaction between two cylindrical inclusions in a symmetric lipid bilayer [J].
Bohinc, K ;
Kralj-Iglic, V ;
May, S .
JOURNAL OF CHEMICAL PHYSICS, 2003, 119 (14) :7435-7444
[9]   Tilted peptides: a motif for membrane destabilization (hypothesis) [J].
Brasseur, R .
MOLECULAR MEMBRANE BIOLOGY, 2000, 17 (01) :31-40
[10]   CHOLESTEROL AND THE GOLGI-APPARATUS [J].
BRETSCHER, MS ;
MUNRO, S .
SCIENCE, 1993, 261 (5126) :1280-1281