Developing a Fluorescence Assay for Monitoring Amyloid-β Aggregation
Alzheimer’s disease is a neurodegenerative disorder that is ranked as the sixth leading cause of death worldwide. The presence of amyloidogenic plaques as well as tau protein fibrils has been implicated in the pathology of the disease. Recent literature has suggested that compounds with antioxidant properties, such as polyphenols, may stifle the aggregation that forms these plaques by reducing oxidative stress. Developing a reliable method for characterizing peptide aggregation would be useful in assessing the effectiveness of these polyphenols. A fluorescence assay utilizing thioflavin T (ThT) was adapted for characterizing the aggregation of different Aβ chains over 14 days. Emission spectra were also collected for multiple polyphenols to determine whether any interaction occurs between the compounds and ThT that might jeopardize assay integrity. Future work will focus on characterizing the aggregation of the peptide in the presence of polyphenols such as nordihydroguaiaretic acid and curcumin.
Keywords: Alzheimer's, Amyloid-ß, Thioflavin T, Polyphenols, Curcumin, Nordihydroguaiaretic Acid, ROS
Topic(s):Chemistry
Biochemistry and Molecular Biology
Biology
Presentation Type: Oral Presentation
Session: TBA
Location: TBA
Time: TBA