Author

Sarah Atali

Date Approved

2021

Date Posted

2021

Degree Type

Campus Only Thesis

Degree Name

Master of Science (MS)

Department

Chemistry

Committee Member

Hedeel Evans, PhD, Chair

Committee Member

Jeffrey Guthrie, PhD

Committee Member

Deborah Heyl-Clegg, PhD

Committee Member

Steven Backues, PhD

Abstract

The importance of amyloid-beta (Aβ) in the development and progression of Alzheimer’s disease (AD) is currently well-recognized. Aβ was recently shown to be protective against certain types of cancer and capable of inhibiting the growth of tumor cells. The mechanisms by which Aβ is converted into functional entities and dysfunctional assemblies are largely obscure. Humanin (HN), a binding partner of Aβ protects against its deleterious effects while acetylcholinesterase (AChE) bound to Aβ peptide, increases aggregation and cytotoxicity of Aβ fibrils. Here, we set out to examine factors that regulate the interactions of Aβ with HN and AChE. We found that ATP, known to decrease misfolding of Aβ, weakened the binding between AChE and Aβ but strengthened the binding between Aβ and HN. When using lung cancer cells conditioned media, we saw more HN was bound to Aβ after ATP addition, while bind of AChE to Aβ was diminished by addition of ATP

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