An alpha-helical peptide in AOT micelles prefers to be localized at the water/headgroup interface.

Abstract:

:A model alpha-helical peptide encapsulated in a reverse micelle is used to study the structure and dynamics of proteins under constrained environments that mimic the membrane-water environment in cells. Molecular dynamics simulations of the self assembly of systems composed of a peptide, sodium bis(2-ethylhexyl) sulfosuccinate (AOT), water, and isooctane show that the peptide prefers to be located at the water/AOT headgroups interface. We explore the effect of the AOT headgroup charge and the peptide charge and find that the peptides migrate to the interface in all cases. These results show that the peptides prefer the constrained hydration environment of the AOT headgroups. The driving force for this configuration is the gain in entropy by released water molecules that otherwise would solvate the protein and surfactant headgroups.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Tian J,Garcia AE

doi

10.1016/j.bpj.2009.03.014

subject

Has Abstract

pub_date

2009-05-20 00:00:00

pages

L57-9

issue

10

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(09)00750-4

journal_volume

96

pub_type

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