Computational Investigation of Polyphenols as Inhibitors to the Aggregation of Amyloid β in Alzheimer’s Disease

Alex P. Platt
Dr. Bill R. Miller, Faculty Mentor

Alzheimer’s Disease (AD) is a degenerative disorder that affects memory retention and damages the brain. AD is the most common form of dementia and a leading cause of death in the United States. One of the main factors in the development of AD is the formation of plaques in the brain, thought to be made of Amyloid β (Aβ), a protein made of 42 residues that gather in peptides and form aggregates. Aβ aggregates in the brain and are stabilized by intermolecular interactions between the individual peptides. Polyphenols are potential inhibitors to this protein aggregation. We use computational methods, such as molecular docking and classical molecular dynamics, to model interactions between Aβ and these polyphenols. This study examines residues 1-16 of Aβ, looking into the structural changes of the model and the binding affinity of each potential inhibitor to this region of the protein structure.

Keywords: Amyloid Beta, Alzheimer's Disease, Computational Chemistry, Moleular Dynamics, Free Energy Calculations

Topic(s):Chemistry

Presentation Type: Oral Presentation

Session: TBA
Location: TBA
Time: TBA