%0 Journal Article
%T Stability of the gramicidin-A channel structure in view of nanofiltration: a computational and experimental study
%+ Nanomédecine, imagerie, thérapeutique - UFC (UR 4662) (NIT / NANOMEDECINE)
%+ Institut Charles Gerhardt Montpellier - Institut de Chimie Moléculaire et des Matériaux de Montpellier (ICGM ICMMM)
%+ Institut Européen des membranes (IEM)
%+ Laboratoire Charles Coulomb (L2C)
%A Bonhenry, D.
%A Kraszewski, S.
%A Picaud, S.
%A Ramseyer, Christophe
%A Balme, Sebastien
%A Janot, Jean-Marc
%A Henn, F.
%< avec comité de lecture
%@ 1744-683X
%J Soft Matter
%I Royal Society of Chemistry
%V 7
%N 22
%P 10651-10659
%8 2011
%D 2011
%R 10.1039/c1sm06277h
%Z Chemical SciencesJournal articles
%X The secondary, ternary and quaternary structures of the biological ion channel Gramicidin-A are investigated by means of UV-visible and fluorescence spectroscopies, and by computational simulations in water/methanol solvent with various molar ratios. Both experiments and molecular dynamics calculations show that the two considered conformations, i.e. the head-to-head and double-stranded β-helix dimers, behave differently with regard to their stability as a function of the methanol content in the water/methanol mixture. To sum-up, calculations show that the double-stranded dimer is stabilized by methanol, even at low content, while the head-to-head dimer conformation breaks into two monomers which remain however coupled whatever the water/methanol mixture. In pure water and low methanol content, the resulting single β-helix structure is maintained due to the stabilization of the channel by water molecules and cations.
%G English
%L hal-00733694
%U https://hal.science/hal-00733694
%~ CNRS
%~ UNIV-FCOMTE
%~ UNIV-MONTP1
%~ UNIV-MONTP2
%~ ENSC-MONTPELLIER
%~ ICG
%~ IEM
%~ L2C
%~ INC-CNRS
%~ MIPS
%~ CHIMIE
%~ UNIV-MONTPELLIER
%~ UM1-UM2
%~ UM-2015-2021