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Structure and dynamics of nano-sized raft-like domains on the plasma membrane

Source: J. Chem. Phys. 136, 015103 (2012); http://dx.doi.org/10.1063/1.3672704

Published 5 January 2012

KEYWORDS and PACS
Keywords
PACS
  • 87.16.dt
    Structure of biomembranes, bilayers and vesicles
  • 87.16.dj
    Dynamics and fluctuations of biomembranes, bilayers and vesicles
  • 87.14.Cc
    Lipids (biomolecules)
  • 87.14.E-
    Proteins
  • YEAR: 2011
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PUBLICATION DATA
ISSN:
1553-9628 (online)
Publisher:
AIP is a member of CrossRef AIP
Fernando E. Herrera1,2 and Sergio Pantano1
1Institut Pasteur de Montevideo, Calle Mataojo 2020, CP 11400 Montevideo, Uruguay
2Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Departamento de Física, Facultad de Bioquímica y Ciencias Biológicas, Universidad Nacional del Litoral, C.C. 242, Ciudad Universitaria, C.P. S3000ZAA, Santa Fe, Argentina
Cell membranes are constitutively composed of thousands of different lipidic species, whose specific organization leads to functional heterogeneities. In particular, sphingolipids, cholesterol and some proteins associate among them to form stable nanoscale domains involved in recognition, signaling, membrane trafficking, etc. Atomic-detail information in the nanometer/second scale is still elusive to experimental techniques. In this context, molecular simulations on membrane systems have provided useful insights contributing to bridge this gap. Here we present the results of a series of simulations of biomembranes representing non-raft and raft-like nano-sized domains in order to analyze the particular structural and dynamical properties of these domains. Our results indicate that the smallest (5 nm) raft domains are able to preserve their distinctive structural and dynamical features, such as an increased thickness, higher ordering, lower lateral diffusion, and specific lipid-ion interactions. The insertion of a transmembrane protein helix into non-raft, extended raft-like, and raft-like nanodomain environments result in markedly different protein orientations, highlighting the interplay between the lipid-lipid and lipid-protein interactions. ©2012 American Institute of Physics
History: Received 4 July 2011; accepted 6 December 2011; published 5 January 2012
Digital Object Identifier: http://dx.doi.org/10.1063/1.3672704

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