Effect of integral proteins in the phase stability of a lipid bilayer: Application to raft formation in cell membranes

被引:17
作者
Gomez, Jordi [1 ]
Sagues, Francesc [1 ]
Reigada, Ramon [1 ]
机构
[1] Univ Barcelona, Dept Quim Fis, E-08028 Barcelona, Spain
关键词
association; biochemistry; biodiffusion; Brownian motion; DNA; molecular biophysics; polymerisation; proteins; reaction kinetics; MONTE-CARLO; GRAPHICAL REPRESENTATIONS; ISING SYSTEMS; ORDER; MICRODOMAINS; CHOLESTEROL; ALGORITHMS; DYNAMICS; DRIVEN; MODEL;
D O I
10.1063/1.3381179
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
We investigate diffusion-limited reactions between a diffusing particle and a target site on a semiflexible polymer, a key factor determining the kinetics of DNA-protein binding and polymerization of cytoskeletal filaments. Our theory focuses on two competing effects: polymer shape fluctuations, which speed up association, and the hydrodynamic coupling between the diffusing particle and the chain, which slows down association. Polymer bending fluctuations are described using a mean field dynamical theory, while the hydrodynamic coupling between polymer and particle is incorporated through a simple heuristic approximation. We validate both of these through comparison to Brownian dynamics simulations. Neither of the effects has been fully considered before in the biophysical context and we show they are necessary to form accurate estimates of reaction processes. The association rate depends on the stiffness of the polymer and the particle size, exhibiting a maximum for intermediate persistence length and a minimum for intermediate particle radius. In the parameter range relevant to DNA-protein binding, the rate increase is up to 100% compared with the Smoluchowski result for simple center-of-mass motion. The quantitative predictions made by the theory can be tested experimentally.
引用
收藏
页数:9
相关论文
共 37 条
[1]   Thermodynamics of membrane domains [J].
Almeida, PFF ;
Pokorny, A ;
Hinderliter, A .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 2005, 1720 (1-2) :1-13
[2]   Cell biology - A role for lipid shells in targeting proteins to caveolae, rafts, and other lipid domains [J].
Anderson, RGW ;
Jacobson, K .
SCIENCE, 2002, 296 (5574) :1821-1825
[3]   Hybrid Lipids as a Biological Surface-Active Component [J].
Brewster, R. ;
Pincus, P. A. ;
Safran, S. A. .
BIOPHYSICAL JOURNAL, 2009, 97 (04) :1087-1094
[4]   Graphical representations for Ising systems in external fields [J].
Chayes, L ;
Machta, J ;
Redner, O .
JOURNAL OF STATISTICAL PHYSICS, 1998, 93 (1-2) :17-32
[5]   Raft domain reorganization driven by short- and long-chain ceramide: A combined AFM and FCS study [J].
Chiantia, Salvatore ;
Kahya, Nicoletta ;
Schwille, Petra .
LANGMUIR, 2007, 23 (14) :7659-7665
[6]   Single-molecule microscopy reveals plasma membrane microdomains created by protein-protein networks that exclude or trap signaling molecules in T cells [J].
Douglass, AD ;
Vale, RD .
CELL, 2005, 121 (06) :937-950
[7]   Cluster Monte Carlo simulations of phase transitions and critical phenomena in zeolites [J].
Dukovski, I ;
Machta, J ;
Saravanan, C ;
Auerbach, SM .
JOURNAL OF CHEMICAL PHYSICS, 2000, 113 (09) :3697-3703
[8]   Influence of nonequilibrium lipid transport, membrane compartmentalization, and membrane proteins on the lateral organization of the plasma membrane [J].
Fan, Jun ;
Sammalkorpi, Maria ;
Haataja, Mikko .
PHYSICAL REVIEW E, 2010, 81 (01)
[9]   Ternary phase diagram of dipalmitoyl-PC/dilauroyl-PC/cholesterol: Nanoscopic domain formation driven by cholesterol [J].
Feigenson, GW ;
Buboltz, JT .
BIOPHYSICAL JOURNAL, 2001, 80 (06) :2775-2788
[10]   A simple mechanism of raft formation in two-component fluid membranes [J].
Foret, L .
EUROPHYSICS LETTERS, 2005, 71 (03) :508-514