Amyloid-ß Oligomer Formations Over Time
Session Number
Project ID: BIO 04
Advisor(s)
Kirsten Viola; Northwestern University
Dr. William Klein; Northwestern University
Discipline
Biology
Start Date
19-4-2023 9:35 AM
End Date
19-4-2023 9:50 AM
Abstract
Alzheimer’s disease is a progressive, and often fatal, disease, and is the leading cause of dementia in older people (Chang et. al, 2003). Based on the amyloid-ß oligomer hypothesis, the brain damage that leads to Alzheimer’s is due to soluble, ligand-like amyloid-ß oligomers (AßOs) (Lambert et. al, 1998, Gong et. al, 2003, Cline et. al, 2018). The aim of this experiment is to understand how time affects the formation of AßOs, specifically at physiological concentrations. Understanding the process of AßO formation will enable us to learn more about how the Aß protein changes from a non-toxic monomer to a neurotoxic oligomer. These experiments use amyloid-beta peptide film to create the samples with a concentration of 30 nanomolar Aß peptide. Eight samples were used, each flash-frozen at a certain time-point after initial sample preparation. A western blot was used to separate and identify the proteins based on the molecular weight of the structure. Results suggest that changes in structure begin at 10 minutes, with the structures organizing into trimers or tetramers after 24 hours. However, difficulty in imaging indicates that future experiments should continue with a higher protein concentration.
Amyloid-ß Oligomer Formations Over Time
Alzheimer’s disease is a progressive, and often fatal, disease, and is the leading cause of dementia in older people (Chang et. al, 2003). Based on the amyloid-ß oligomer hypothesis, the brain damage that leads to Alzheimer’s is due to soluble, ligand-like amyloid-ß oligomers (AßOs) (Lambert et. al, 1998, Gong et. al, 2003, Cline et. al, 2018). The aim of this experiment is to understand how time affects the formation of AßOs, specifically at physiological concentrations. Understanding the process of AßO formation will enable us to learn more about how the Aß protein changes from a non-toxic monomer to a neurotoxic oligomer. These experiments use amyloid-beta peptide film to create the samples with a concentration of 30 nanomolar Aß peptide. Eight samples were used, each flash-frozen at a certain time-point after initial sample preparation. A western blot was used to separate and identify the proteins based on the molecular weight of the structure. Results suggest that changes in structure begin at 10 minutes, with the structures organizing into trimers or tetramers after 24 hours. However, difficulty in imaging indicates that future experiments should continue with a higher protein concentration.