Thioflavin T Binding to Amyloid Fibrils

Treatment of Alzheimer’s disease (AD) is hampered by the fact that the disease progression cannot be tracked in vivo at this time. Understanding the properties of Aβ amyloid fibrils associated with AD is imperative to finding a way to track the progression of the disease. Recently, fluorescent markers, derived from thioflavin T have been developed as markers of AD. This project examines the intrinsic fluorescence of thioflavin T as well as the fluorescence of thioflavin T bound to Aβ(1-40) amyloid fibrils with two distinct morphologies. The two fibril polymorphs produced different fluorescence emission intensities. The goal is to better understand the structural and binding properties of these amyloid fibrils in an attempt to provide earlier diagnosis of amyloid disorders, specifically AD. Introduction Amyloid is a type of insoluble fibrous protein aggregate. Amyloid fibrils play a role in some normal processes in the body, such as melanin formation. Amyloid, however, can accumulate in such a manner as to inhibit or degrade normal cellular function. Abnormal amyloid accumulations are frequently present in some neurodegenerative diseases, such as Alzheimer’s disease (AD). The study of amyloid peptide aggregation and accumulation as amyloid plaques has become a priority in research that spans a multitude of academic disciplines. The connection between