36th Annual Student Research Conference
Computational Investigation of Polyphenols on the Disaggregation of Amyloid β (1-40) as a Treatment for Alzheimer’s Disease
Hannah C. Zimmerman
Dr. Bill R. Miller, Faculty Mentor
Alzheimer’s Disease (AD) is a neurodegenerative disease that results in the degradation of the brain and is a leading cause of death. The Amyloid β hypothesis for AD proposes that the Amyloid β protein (Aβ) can aggregate to form plaques in the brain. Aβ is mainly stabilized by hydrogen bonding in a β-sheet conformation. 15 polyphenol drugs are being investigated for Aβ(1-40) disaggregation potential alongside Thioflavin T (ThT), a fluorescent dye used to quantify disaggregation in experimental labs. Computational techniques including molecular docking and molecular dynamics (MD) simulations were used to model protein-drug interactions. Structural, energetic, and hydrogen bond analyses were performed to investigate these interactions. Gossypetin (GOS) is a promising drug that appears to correspond with a decreased β-sheet composition, increased movement, and decreased backbone hydrogen bonding of the Aβ protein showing promise as a potential AD inhibitor in silico.
Keywords: Alzheimer's Disease, Molecular Dynamics, Disaggregation, Molecular Docking, Amyloid Beta, Computational, Biochemistry, Hydrogen Bonding
Topic(s):Biochemistry and Molecular Biology
Chemistry
Biology
Presentation Type: Oral Presentation
Session: 108-3
Location: MG 1000
Time: 9:00