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Title: Inhibition of beta-amyloid aggregation by fluorescent dye labels

Journal Article · · Applied Physics Letters
DOI:https://doi.org/10.1063/1.4865197· OSTI ID:22283163

The fluorescence decay of beta-amyloid's (Aβ) intrinsic fluorophore tyrosine has been used for sensing the oligomer formation of dye-labelled Aβ monomers and the results compared with previously studied oligomerization of the non-labelled Aβ peptides. It has been demonstrated that two different sized, covalently bound probes 7-diethylaminocoumarin-3-carbonyl and Hilyte Fluor 488 (HLF), alter the rate and character of oligomerization to different extents. The ability of HLF to inhibit formation of highly ordered structures containing beta-sheets was also shown. The implications of our findings for using fluorescence methods in amyloidosis research are discussed and the advantages of this auto-fluorescence approach highlighted.

OSTI ID:
22283163
Journal Information:
Applied Physics Letters, Vol. 104, Issue 6; Other Information: (c) 2014 AIP Publishing LLC; Country of input: International Atomic Energy Agency (IAEA); ISSN 0003-6951
Country of Publication:
United States
Language:
English

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