Date Approved
2021
Date Posted
2021
Degree Type
Campus Only Thesis
Degree Name
Master of Science (MS)
Department or School
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
Recommended Citation
Atali, Sarah, "Examining the binding of humanin and acetylcholinesterase with amyloid beta" (2021). Master's Theses and Doctoral Dissertations. 1077.
https://commons.emich.edu/theses/1077