Lipid lateral mobility and membrane phase structure modulation by protein binding

Martin B. Forstner, Chanel K. Yee, Atul N. Parikh, Jay T. Groves

Research output: Contribution to journalArticle

72 Scopus citations

Abstract

Using a combination of fluorescence correlation and infrared absorption spectroscopies, we characterize lipid lateral diffusion and membrane phase structure as a function of protein binding to the membrane surface. In a supported membrane configuration, cholera toxin binding to the pentasaccharaide headgroup of membrane-incorporated GM1 lipid alters the long-range lateral diffusion of fluorescently labeled probe lipids, which are not involved in the binding interaction. This effect is prominently amplified near the gel-fluid transition temperature, Tm, of the majority lipid component. At temperatures near Tm, large changes in probe lipid diffusion are measured at average protein coverage densities as low as 0.02 area fraction. Spectral shifts of the methylene symmetric and asymmetric stretching modes in the lipid acyl chain confirm that protein binding alters the fraction of lipid in the gel phase.

Original languageEnglish (US)
Pages (from-to)15221-15227
Number of pages7
JournalJournal of the American Chemical Society
Volume128
Issue number47
DOIs
StatePublished - Nov 29 2006

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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