Fluorescence quenching by lipid encased nanoparticles shows that amyloid-β has a preferred orientation in the membrane

Chem Commun (Camb). 2018 Jul 10;54(56):7750-7753. doi: 10.1039/c8cc02108b.

Abstract

Short range plasmonic fields around a nanoparticle can modulate fluorescence or Raman processes. In lipid encased nanoparticles, this can potentially measure the relative depths of different parts of a membrane protein from the surface. We employ this technique to discover that membrane inserted amyloid-β oligomers have a preferred molecular orientation.

MeSH terms

  • Amyloid beta-Peptides / chemical synthesis
  • Amyloid beta-Peptides / chemistry*
  • Cholesterol / chemistry
  • Fluoresceins / chemistry
  • Fluorescence
  • Fluorescent Dyes / chemistry
  • Lipid Bilayers / chemistry*
  • Metal Nanoparticles / chemistry*
  • Peptide Fragments / chemical synthesis
  • Peptide Fragments / chemistry*
  • Phosphatidylcholines / chemistry
  • Phosphatidylglycerols / chemistry
  • Silver / chemistry
  • Spectrometry, Fluorescence
  • Spectrum Analysis, Raman

Substances

  • Amyloid beta-Peptides
  • Fluoresceins
  • Fluorescent Dyes
  • Lipid Bilayers
  • Peptide Fragments
  • Phosphatidylcholines
  • Phosphatidylglycerols
  • amyloid beta-protein (1-40)
  • Silver
  • 1-palmitoyl-2-oleoylglycero-3-phosphoglycerol
  • Cholesterol
  • 1-palmitoyl-2-oleoylphosphatidylcholine