Behavior of maltose-neopentyl glycol-3 (MNG-3) at the air/aqueous interface

被引:0
|
作者
Yoo, Bowon [1 ,2 ]
Lee, Jisun [1 ,2 ]
Choi, Soyoung [1 ,2 ]
Ryu, Jungju [1 ,2 ]
Lee, Hoik [1 ,2 ]
Chae, Pil Seok [3 ]
Lee, Sang Uck [4 ]
Maeda, Mizuo [5 ]
Sohn, Daewon [1 ,2 ]
机构
[1] Dept Chem, Seoul 133791, South Korea
[2] Res Inst Convergence Basic Sci, Seoul 133791, South Korea
[3] Hanyang Univ, Dept Bionanotechnol, Ansan 426791, South Korea
[4] Hanyang Univ, Dept Appl Chem, Ansan 426791, South Korea
[5] RIKEN, Bioengn Lab, Wako, Saitama 3510198, Japan
基金
新加坡国家研究基金会;
关键词
Integral membrane proteins; Protein surfactant; MNG-3; Langmuir-Schaefer film; X-ray reflectivity; Surface pressure-area isotherm; ATOMIC-FORCE MICROSCOPY; MEMBRANE-PROTEINS; STABILIZATION; MODEL; CRYSTALLIZATION; SOLUBILIZATION; AMPHIPHILES; FILMS;
D O I
10.1016/j.colsurfa.2015.07.054
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
Integral membrane proteins (IMPS) performing a variety of cell functions comprise a significant fraction of the proteins encoded in an organism's genome. Maltose-neopentyl glycol-3 (MNG-3) was invented as a novel detergent to extract IMPs from the cell membranes; MNG-3 has an inherent flexibility originating from its central carbon and its arms comprising alkyl chains and maltose groups. Herein, we demonstrate the reverse-scissoring behavior of MNG-3 through the use of different subphase conditions at the air/water interface. The origin of its high performance was investigated by means of Langmuir techniques, X-ray reflectivity (XRR) analysis of its Langmuir-Schaefer (LS) film, Brewster angle microscope (BAM) and atomic force microscope (AFM) and computational simulation. (C) 2015 Elsevier B.V. All rights reserved.
引用
收藏
页码:184 / 189
页数:6
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