Cytochrome c interaction with neutral lipid membranes: influence of lipid packing and protein charges

被引:9
作者
El Kirat, Karim [2 ]
Morandat, Sandrine [1 ]
机构
[1] Univ Technol Compiegne, CNRS, UMR 6022, Lab Genie Enzymat & Cellulaire, F-60205 Compiegne, France
[2] Univ Technol Compiegne, CNRS, UMR 6600, Lab Biomecan & Bioingn, F-60205 Compiegne, France
关键词
Biomimetic membranes; Cytochrome c; Atomic force microscopy; Time-lapse AFM; Model lipid membranes; ATOMIC-FORCE MICROSCOPY; SUPPORTED PHOSPHATIDYLCHOLINE BILAYERS; POLYCATIONIC POLYMERS; PHOSPHOLIPID-BILAYERS; PERIPHERAL PROTEINS; DOMAINS; PEPTIDE; CARDIOLIPIN; ELECTRODES; RESONANCE;
D O I
10.1016/j.chemphyslip.2009.08.002
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
The interaction of cytochrome c (cyt c) with fluid/gel neutral supported lipid membranes was investigated by time-lapse atomic force microscopy (AFM). AFM revealed the random formation of depressed areas in fluid membranes promoted by cyt c. These depressions corresponded to the desorption of fluid bilayer patches induced by cyt c. By contrast, the gel domains were never desorbed but they were progressively thickened in the presence of the protein. These results suggest that cyt c molecules might intercalate between the mica and the lipid bilayer. Although the interaction of cyt c with the mica surface is likely to be an artifact, this work is the first direct observation of cyt c ability to cross membranes. Furthermore, our data show that the net positive charge of cyt c molecules plays a pivotal role but it is not the sole factor responsible for cyt c insertion in the membrane. (C) 2009 Elsevier Ireland Ltd. All rights reserved.
引用
收藏
页码:17 / 24
页数:8
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