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

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 amy...

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Bibliographic Details
Published in:Chemical communications (Cambridge, England) England), 2018, Vol.54 (56), p.7750-7753
Main Authors: Chandra, Bappaditya, Maity, Barun Kumar, Das, Anirban, Maiti, Sudipta
Format: Article
Language:English
Subjects:
Amyloid beta-Peptides - chemical synthesis
Amyloid beta-Peptides - chemistry
Cholesterol - chemistry
Fluoresceins - chemistry
Fluorescence
Fluorescent Dyes - chemistry
Lipid Bilayers - chemistry
Metal Nanoparticles - chemistry
Molecular chains
Nanoparticles
Oligomers
Peptide Fragments - chemical synthesis
Peptide Fragments - chemistry
Phosphatidylcholines - chemistry
Phosphatidylglycerols - chemistry
Preferred orientation
Proteins
Silver - chemistry
Spectrometry, Fluorescence
Spectrum Analysis, Raman
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Summary: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.
ISSN:1359-7345
1364-548X
DOI:10.1039/c8cc02108b