37th Annual Student Research Conference
A computational investigation of the effects polyphenol drugs have on the inhibition of Amyloid Beta aggregates in association with Alzheimer’s Disease
Kaiden J. Zaborowski
Dr. Bill R. Miller, Faculty Mentor
Alzheimer’s disease (AD), a neurodegenerative condition, is the sixth leading cause of death in those 65 and older in the US. The leading hypothesis for its causation is the aggregation of Amyloid-β peptides. Amyloid-β is a short, 42 amino acid peptide that forms a horseshoe beta sheet structure that is characteristic of the fibril formation. These aggregates have been shown to decrease synapse number and depress synapse activity. In the current study, we employ computational chemistry methods, such as molecular docking and molecular dynamics, to describe the mechanisms behind drug inhibition and Amyloid-β disaggregation. Specifically, we are investigating the interaction between the Amyloid-β Protein and the stilbenoids myricetin and pterostilbene. Stilbenoids show promise as Amyloid-β aggregation inhibitors because of the interaction between their hydroxyl groups and aggregated beta sheets. Analysis of our simulations will hopefully provide new information on disaggregation of Amyloid-β by polyphenols as potential treatments for Alzheimer’s disease.
Keywords: Computational, Chemistry, Inhibitor, Medicine, Medical, Biology, Disaggregation, Synapse
Topic(s):Chemistry
Presentation Type: Oral Presentation
Session: 106-3
Location: MG 2001
Time: 9:45