Dynamics of Membrane Proteins within Synthetic Polymer Membranes with Large Hydrophobic Mismatch

被引：97
作者：
Itel, Fabian [1 ]
Najer, Adrian [1 ]
Palivan, Cornelia G. [1 ]
Meier, Wolfgang [1 ]
机构：
[1] Univ Basel, Dept Chem, CH-4056 Basel, Switzerland
来源：
NANO LETTERS | 2015年 / 15卷 / 06期
基金：
瑞士国家科学基金会;
关键词：
Membrane proteins; lateral diffusion; synthetic membranes; hydrophobic mismatch; fluorescence correlation spectroscopy; amphiphilic block copolymers; FLUORESCENCE CORRELATION SPECTROSCOPY; ANOMALOUS SUBDIFFUSION; LATERAL DIFFUSION; COPOLYMER MEMBRANES; BILAYER THICKNESS; LIPID-MEMBRANES; NANOREACTORS; NANOCOMPARTMENTS; RECONSTITUTION; MOBILITY;
D O I：
10.1021/acs.nanolett.5b00699
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
The functioning of biological membrane proteins (MPs) within synthetic block copolymer membranes is an intriguing phenomenon that is believed to offer great potential for applications in life and medical sciences and engineering. The question why biological MPs are able to function in this completely artificial environment is still unresolved by any experimental data. Here, we have analyzed the lateral diffusion properties of different sized MPs within poly(dimethylsiloxane) (PDMS)-containing amphiphilic block copolymer membranes of membrane thicknesses between 9 and 13 nm, which results in a hydrophobic mismatch between the membrane thickness and the size of the proteins of 3.3-7.1 nm (3.5-5 times). We show that the high flexibility of PDMS, which provides membrane fluidities similar to phospholipid bilayers, is the key-factor for MP incorporation.
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收藏
页码：3871 / 3878
页数：8
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