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. (C) 2015 Elsevier B.V. All rights reserved.