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

Bowon Yoo; Jisun Lee; Soyoung Choi; Jungju Ryu; Hoik Lee; Pil Seok Chae; Sang Uck Lee; Mizuo Maeda; Daewon Sohn

doi:10.1016/j.colsurfa.2015.07.054

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

Bowon Yoo
, Jisun Lee
, Soyoung Choi
, Jungju Ryu
, Hoik Lee
, Pil Seok Chae
, Sang Uck Lee
, Mizuo Maeda
, Daewon Sohn

Department of Chemistry and Research Institute for Convergence of Basic Science
Hanyang University
RIKEN

Research output: Contribution to journal › Article › peer-review

Abstract

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.

Original language	English
Pages (from-to)	184-189
Number of pages	6
Journal	Colloids and Surfaces A: Physicochemical and Engineering Aspects
Volume	484
DOIs	https://doi.org/10.1016/j.colsurfa.2015.07.054
State	Published - 5 Nov 2015
Externally published	Yes

Keywords

Integral membrane proteins
Langmuir-Schaefer film
MNG-3
Protein surfactant
Surface pressure-area isotherm
X-ray reflectivity

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10.1016/j.colsurfa.2015.07.054

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

abstract = "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.",

keywords = "Integral membrane proteins, Langmuir-Schaefer film, MNG-3, Protein surfactant, Surface pressure-area isotherm, X-ray reflectivity",

author = "Bowon Yoo and Jisun Lee and Soyoung Choi and Jungju Ryu and Hoik Lee and Chae, \{Pil Seok\} and Lee, \{Sang Uck\} and Mizuo Maeda and Daewon Sohn",

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year = "2015",

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doi = "10.1016/j.colsurfa.2015.07.054",

language = "English",

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T1 - Behavior of maltose-neopentyl glycol-3 (MNG-3) at the air/aqueous interface

AU - Yoo, Bowon

AU - Lee, Jisun

AU - Choi, Soyoung

AU - Ryu, Jungju

AU - Lee, Hoik

AU - Chae, Pil Seok

AU - Lee, Sang Uck

AU - Maeda, Mizuo

AU - Sohn, Daewon

PY - 2015/11/5

Y1 - 2015/11/5

N2 - 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.

AB - 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.

KW - Integral membrane proteins

KW - Langmuir-Schaefer film

KW - MNG-3

KW - Protein surfactant

KW - Surface pressure-area isotherm

KW - X-ray reflectivity

UR - https://www.scopus.com/pages/publications/84939449797

U2 - 10.1016/j.colsurfa.2015.07.054

DO - 10.1016/j.colsurfa.2015.07.054

M3 - Article

AN - SCOPUS:84939449797

SN - 0927-7757

VL - 484

SP - 184

EP - 189

JO - Colloids and Surfaces A: Physicochemical and Engineering Aspects

JF - Colloids and Surfaces A: Physicochemical and Engineering Aspects

ER -

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

Abstract

Keywords

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