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

• Published in: Colloids and surfaces. A, Physicochemical and engineering aspects Physicochemical and engineering aspects, 2015-11, Vol.484, p.184-189
• Main Authors: Yoo, Bowon, Lee, Jisun, Choi, Soyoung, Ryu, Jungju, Lee, Hoik, Chae, Pil Seok, Lee, Sang Uck, Maeda, Mizuo, Sohn, Daewon
• Format: Article
• Language: English
• Subjects: Integral membrane proteins; Langmuir–Schaefer film; MNG-3; Protein surfactant; Surface pressure-area isotherm; X-ray reflectivity
• ISSN: 0927-7757; 1873-4359
• DOI: 10.1016/j.colsurfa.2015.07.054

[Display omitted] •Maltose-neopentyl glycol-3 (MNG-3) is a detergent to extract proteins from the cell.•Determined the mechanism of MNG-3 as a protein-solubilizing agent at the interface.•MNG-3 for extracting membrane proteins arises from the reverse-scissoring movement. 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.