The essential focus of this research is to study the structure of amyloid � (A�) fibril aggregates constituting characteristic extracellular senile plaques detected in the brains of Alzheimer's patients, as well as the mechanism of aggregation (particularly the initial stages of the mechanism). This analysis is executed by utilization of enhanced Thioflavin � T (ThT) fluorescence upon binding amyloid � fibrils. We investigate the spectra in an attempt to assign potential conformations of amyloid fibrils to the observed fluorescence peaks. We found that ThT fluorescence was enhanced at basic solution conditions with the presence of A �. Furthermore, we investigated the fluorescence lifetime of the ThT conjugated A� in order to characterize the dynamics of ThT influenced by the conformation of A�.

ThT fluorescence study on aggregation of A� peptides

248th National Meeting (2014)

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