Inhibition of beta-amyloid aggregation by fluorescent dye labels

Amaro, Mariana and Wellbrock, Thorben and Birch, David and Rolinski, Olaf (2014) Inhibition of beta-amyloid aggregation by fluorescent dye labels. Applied Physics Letters, 104 (6). 063704. ISSN 0003-6951 (

[thumbnail of Ab-manuscript] Microsoft Word. Filename: Ab_manuscript.docx

Download (58kB)


The fluorescence decay of beta-amyloid’s (Ab) intrinsic fluorophore tyrosine has been used for sensing the oligomer formation of dye-labelled Ab monomers and the results compared with previously studied oligomerization of the non-labelled Ab 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.