Date of Graduation
5-2018
Document Type
Thesis
Degree Name
Bachelor of Science in Chemical Engineering
Degree Level
Undergraduate
Department
Chemical Engineering
Advisor/Mentor
Hestekin, Christa
Abstract
Alzheimer’s disease is the only disease in the ten leading causes of death in the United states that cannot be slowed, prevented, or cured. Alzheimer’s dementia and type II diabetes are the top two diseases caused by improper protein folding, aggregation, and deposition of fibrillar plaques in tissues. These plaques, originally thought to be the cause of these diseases, have been discovered to be mostly benign and representative of the later stages of the disease. The smaller, more soluble oligomeric aggregates are responsible for the death of pancreatic and neural cells. Many oligomeric species are unstable and exist only for a short period of time, which makes them difficult to study. Photo-induced cross-linking of unmodified proteins (PICUP) is a method that allows researchers to take “snapshots” of an aggregation as it progresses. In this study, PICUP is used to study two proteins, amyloid beta and amylin, which are involved in the continuation of Alzheimer’s dementia and type II diabetes. Both proteins were successfully cross-linked and visualized on polyacrylamide gels using silver staining techniques. Amyloid beta aggregation in sodium phosphate and HEPES buffers were also compared and showed similar aggregation between the two.
Keywords
protein, amyloid, aggregate, alzheimer's, diabetes
Citation
Booth, G. (2018). Cross-linking Amyloid Forming Proteins for Improved Understanding of Early Aggregation. Chemical Engineering Undergraduate Honors Theses Retrieved from https://scholarworks.uark.edu/cheguht/125