Aggregation Process of Amyloid Peptides in Alzheimer's Disease
School Name
South Carolina Governor's School for Science and Mathematics
Grade Level
12th Grade
Presentation Topic
Biochemistry
Presentation Type
Mentored
Abstract
Alzheimer's disease (AD) is a neurodegenerative disorder that is believed to begin early in a patient's life and continues to progress into old age. The amyloid hypothesis postulates that the accumulation of amyloid β (Aβ) plaques and soluble Aβ oligomers are the primary cause of AD. Because there is no cure for AD and it is a progressive disease, it is desirable to study the aggregation of Aβ in order to provide preventative actions and early treatment. Our study focuses on mapping the aggregation dynamics of Aβ peptides using a nanopore biosensor. Due to the unpredictable nature of the α-Hemolysin (αHL) protein, the nanopore's stability varies widely. Because of this, we were unable to collect the number of events needed to have statistically significant data within six weeks. However, after passing analytes through the αHL pore, we expect each Aβ species (Aβ 40 monomers, oligomers, and soluble aggregates) to display unique signal characteristics. We predict that Aβ monomers will show a long dwell time and full current blockage. In contrast, oligomers and larger soluble aggregates will show brief, partial current blockades. After studying these aggregation dynamics, our research will continue by seeing the effect of cannabinoid drugs on the Aβ aggregation dynamics. We hope to provide quantitative analysis to determine their effectiveness as a treatment for AD using quantitative analysis.
Recommended Citation
Brown, Nyasia, "Aggregation Process of Amyloid Peptides in Alzheimer's Disease" (2023). South Carolina Junior Academy of Science. 2.
https://scholarexchange.furman.edu/scjas/2023/all/2
Location
ECL 115
Start Date
3-25-2023 10:45 AM
Presentation Format
Oral Only
Group Project
No
Aggregation Process of Amyloid Peptides in Alzheimer's Disease
ECL 115
Alzheimer's disease (AD) is a neurodegenerative disorder that is believed to begin early in a patient's life and continues to progress into old age. The amyloid hypothesis postulates that the accumulation of amyloid β (Aβ) plaques and soluble Aβ oligomers are the primary cause of AD. Because there is no cure for AD and it is a progressive disease, it is desirable to study the aggregation of Aβ in order to provide preventative actions and early treatment. Our study focuses on mapping the aggregation dynamics of Aβ peptides using a nanopore biosensor. Due to the unpredictable nature of the α-Hemolysin (αHL) protein, the nanopore's stability varies widely. Because of this, we were unable to collect the number of events needed to have statistically significant data within six weeks. However, after passing analytes through the αHL pore, we expect each Aβ species (Aβ 40 monomers, oligomers, and soluble aggregates) to display unique signal characteristics. We predict that Aβ monomers will show a long dwell time and full current blockage. In contrast, oligomers and larger soluble aggregates will show brief, partial current blockades. After studying these aggregation dynamics, our research will continue by seeing the effect of cannabinoid drugs on the Aβ aggregation dynamics. We hope to provide quantitative analysis to determine their effectiveness as a treatment for AD using quantitative analysis.
