Journal
ANALYTICAL CHEMISTRY
Volume 92, Issue 7, Pages 4963-4970Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.analchem.9b05092
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- University of Zurich
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The amyloid-beta peptide is correlated with Alzheimer's disease and is assumed to cause toxicity by its interaction with the neuron membrane. A custom-made microscope objective based on the supercritical angle technique was developed by our group, which allows investigation of interfacial events by performing surface-sensitive and low-invasive spectroscopy. Applied to Raman spectroscopy, this technique was used to collect information about the structure of polypeptides that interact with a supported lipid bilayer. Notably, the conformation used by amyloid-beta(1-40) and amyloid-beta(1-42) when interacting directly with or next to the supported lipid bilayer was characterized. We observed two distinct secondary structures, alpha-helix and beta-sheet, which were exhibited by the peptide. These two structures were detected simultaneously. The propensity of the peptide to fold into these structures seemed dependent on both their number of amino acids and their proximity with the supported lipid bilayer. The alpha-helix structure was observed for amyloid-beta(1-42) fragments that were closer to the lipid bilayer. Peptides that were located further away from the bilayer favored the beta-sheet structure. Amyloid-beta(1-40) was less prone to adopt the alpha-helix secondary structure.
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