Fluorescent N-arylaminonaphthalene sulfonate probes for amyloid aggregation of alpha-synuclein.

CELEJ MS; JARES-ERIJMAN EA; JOVIN TM.

Biophysical Society

Lugar: USA; Año: 2008 vol. 94 p. 4867 - 4867

The deposition of fibrillar structures (amyloids) is characteristic of pathological conditions including Alzheimer’s and Parkinson’s diseases. The detection of protein deposits and the evaluation of their kinetics of aggregation are generally based on fluorescent probes such as thioflavin T and Congo red. In a search for improved fluorescence tools for studying amyloid formation, we explored the ability of N-arylaminonaphthalene sulfonate (NAS) derivatives to act as noncovalent probes of a-synuclein (AS) fibrillation, a process linked to Parkinson’s disease and other neurodegenerative disorders. The compounds bound to fibrillar AS with micromolar Kds, and exhibited fluorescence enhancement, hyperchromism, and high anisotropy. Weconclude that the probes experience a hydrophobic environment and/or restricted motion in a polar region. Time- and spectrally resolved emission intensity and anisotropy provided further information regarding structural features of the protein and the