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

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.
Authors:
; ; ;  [1]
  1. Photophysics group, Centre for Molecular Nanometrology, Department of Physics, Scottish Universities Physics Alliance, University of Strathclyde, 107 Rottenrow, Glasgow G4 0NG (United Kingdom)
Publication Date:
OSTI Identifier:
22283163
Resource Type:
Journal Article
Resource Relation:
Journal Name: Applied Physics Letters; Journal Volume: 104; Journal Issue: 6; Other Information: (c) 2014 AIP Publishing LLC; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; 75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; AGGLOMERATION; CARBONYLS; COMPARATIVE EVALUATIONS; COVALENCE; DYES; FLUORESCENCE; MONOMERS; PEPTIDES; PHOSPHORS; TYROSINE