Beyond Saffman-Delbruck approximation: A new regime for 2D diffusion of α-hemolysin complexes in supported lipid bilayer

被引:10
作者
Harb, Frederic [1 ]
Sarkis, Joe [1 ,2 ]
Ferte, Natalie [1 ]
Tinland, Bernard [1 ]
机构
[1] Aix Marseille Univ, CNRS, UMR7325, CINaM, F-13288 Marseille, France
[2] Lyon Univ Lyon 1 CPE Lyon, UMR CNRS INSA 5246, Inst Chim & Biochim Mol & Supramol, Equipe GEMBAS, Villeurbanne, France
关键词
PORE-FORMING PROTEIN; INTEGRAL MEMBRANE-PROTEINS; LATERAL DIFFUSION; FLUORESCENCE RECOVERY; ESCHERICHIA-COLI; ION CHANNELS; RECONSTITUTION; MOBILITY; TOXIN; MODULATION;
D O I
10.1140/epje/i2012-12118-6
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
Cell mechanisms are actively modulated by membrane dynamics. We studied the dynamics of a first-stage biomimetic system by Fluorescence Recovery After Patterned Photobleaching. Using this simple biomimetic system, constituted by alpha-hemolysin from Staphylococcus aureus inserted as single heptameric pore or complexes of pores in a glass-supported DMPC bilayer, we observed true diffusion behavior, with no immobile fraction. We find two situations: i) when incubation is shorter than 15 hours, the protein inserts as a heptameric pore and diffuses roughly three times more slowly than its host lipid bilayer; ii) incubation longer than 15 hours leads to the formation of larger complexes which diffuse more slowly. Our results indicate that, while the Saffman-Delbruck model adequately describes the diffusion coefficient D for small radii, D of the objects decreases as 1/R-2 for the size range explored in this study. Additionally, in the presence of inserted proteins, the gel-to-fluid transition of the supported bilayer as well as a temperature shift in the gel-to-fluid transition are observed.
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页数:9
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共 66 条
[1]   SELF-DIFFUSION OF INTERACTING MEMBRANE-PROTEINS [J].
ABNEY, JR ;
SCALETTAR, BA ;
OWICKI, JC .
BIOPHYSICAL JOURNAL, 1989, 55 (05) :817-833
[2]   Microsecond time-scale discrimination among polycytidylic acid, polyadenylic acid, and polyuridylic acid as homopolymers or as segments within single RNA molecules [J].
Akeson, M ;
Branton, D ;
Kasianowicz, JJ ;
Brandin, E ;
Deamer, DW .
BIOPHYSICAL JOURNAL, 1999, 77 (06) :3227-3233
[3]   Imaging α-hemolysin with molecular dynamics:: Ionic conductance, osmotic permeability, and the electrostatic potential map [J].
Aksimentiev, A ;
Schulten, K .
BIOPHYSICAL JOURNAL, 2005, 88 (06) :3745-3761
[4]   USE OF A FLUORESCENT CHOLESTEROL DERIVATIVE TO MEASURE LATERAL MOBILITY OF CHOLESTEROL IN MEMBRANES [J].
ALECIO, MR ;
GOLAN, DE ;
VEATCH, WR ;
RANDO, RR .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES, 1982, 79 (17) :5171-5174
[5]   Reversible adsorption and nonreversible insertion of Escherichia coli alpha-hemolysin into lipid bilayers [J].
Bakas, L ;
Ostolaza, H ;
Vaz, WLC ;
Goni, FM .
BIOPHYSICAL JOURNAL, 1996, 71 (04) :1869-1876
[6]   STAPHYLOCOCCAL ALPHA-TOXIN - OLIGOMERIZATION OF HYDROPHILIC MONOMERS TO FORM AMPHIPHILIC HEXAMERS INDUCED THROUGH CONTACT WITH DEOXYCHOLATE DETERGENT MICELLES [J].
BHAKDI, S ;
FUSSLE, R ;
TRANUMJENSEN, J .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES, 1981, 78 (09) :5475-5479
[7]   α-Hemolysin pore formation into a supported phospholipid bilayer using cell-free expression [J].
Chalmeau, Jerome ;
Monina, Nadezda ;
Shin, Jonghyeon ;
Vieu, Christophe ;
Noireaux, Vincent .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 2011, 1808 (01) :271-278
[8]   Adsorbed and free lipid bilayers at the solid-liquid interface [J].
Charitat, T ;
Bellet-Amalric, E ;
Fragneto, G ;
Graner, F .
EUROPEAN PHYSICAL JOURNAL B, 1999, 8 (04) :583-593
[9]   Main phase transitions in supported lipid single-bilayer [J].
Charrier, A ;
Thibaudau, F .
BIOPHYSICAL JOURNAL, 2005, 89 (02) :1094-1101
[10]   Staphylococcal α-hemolysin can form hexamers in phospholipid bilayers [J].
Czajkowsky, DM ;
Sheng, ST ;
Shao, ZF .
JOURNAL OF MOLECULAR BIOLOGY, 1998, 276 (02) :325-330