Interaction of diverse voltage sensor homologs with lipid bilayers revealed by self-assembly simulations

Younes Mokrab, Mark S P Sansom

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

Voltage sensors (VS) domains couple the activation of ion channels/enzymes to changes in membrane voltage. We used molecular dynamics simulations to examine interactions with lipids of several VS homologs. VSs in intact channels in the activated state are exposed to phospholipids, leading to a characteristic local distortion of the lipid bilayer which decreases its thickness by ∼10 Å. This effect is mediated by a conserved hydrophilic stretch in the S4-S5 segment linking the VS and the pore domains, and may favor gating charges crossing the membrane. In cationic lipid bilayers lacking phosphate groups, VSs form fewer contacts with lipid headgroups. The S3-S4 paddle motifs show persistent interactions of individual lipid molecules, influenced by the hairpin loop. In conclusion, our results suggest common interactions with phospholipids for various VS homologs, providing insights into the molecular basis of their stabilization in the membrane and how they are altered by lipid modification.

Original languageEnglish
Pages (from-to)875-884
Number of pages10
JournalBiophysical Journal
Volume100
Issue number4
DOIs
Publication statusPublished - 16 Feb 2011
Externally publishedYes

Fingerprint

Lipid Bilayers
Lipids
Phospholipids
Membranes
Molecular Dynamics Simulation
Membrane Lipids
Ion Channels
Phosphates
Enzymes

ASJC Scopus subject areas

  • Biophysics

Cite this

Interaction of diverse voltage sensor homologs with lipid bilayers revealed by self-assembly simulations. / Mokrab, Younes; Sansom, Mark S P.

In: Biophysical Journal, Vol. 100, No. 4, 16.02.2011, p. 875-884.

Research output: Contribution to journalArticle

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