Examining the binding of humanin and acetylcholinesterase with amyloid beta

<p>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</p>

Name thesis:degree_name

Master of Science (MS)

Level thesis:degree_level

Campus Only Thesis

Discipline thesis:degree_discipline

Chemistry

Year dc:date.available

2021

Author dc:creator

• Atali, Sarah

Contributors dc:contributor

• Hedeel Evans, PhD, Chair
• Jeffrey Guthrie, PhD
• Deborah Heyl-Clegg, PhD

• Chemistry

Repository record dc:identifier

https://commons.emich.edu/theses/1077

OAI identifier oai:identifier

oai:commons.emich.edu:theses-2451