Date of Graduation
5-2016
Document Type
Thesis
Degree Name
Bachelor of Science in Biomedical Engineering
Degree Level
Undergraduate
Department
Biomedical Engineering
Advisor/Mentor
Hestekin, Christa
Committee Member/Reader
Jensen, Hanna
Committee Member/Second Reader
Zaharoff, David
Abstract
Amyloid Beta (Aβ) was the major focus of this study. It is a peptide that is present in the brain with a high tendency to self-aggregate. When this protein aggregates, it forms oligomers and protofibrils which in turn are deposited as senile plaques in the brain. The reason for the concern with these plaques is their association with the neurological disorder Alzheimer’s disease. It has been found that the most dangerous oligomers are formed in a portion of the plasma membrane known as lipid rafts. The purpose of this study was to understand how micelles affect the aggregation properties of Aβ. To model the lipid rafts in the brain, micelles formed from DHPC and DMPC were used. Aβ and these micelles were separated using micellular electrokinetic chromatography (MEKC). It was determined that micelles in sodium phosphate buffer could successfully be detected by MEKC. It was also determined that Aβ and the micelles migrate in opposite directions during capillary electrophoresis. With the success of further experimentation, more will be known about the way that the lipids rafts in the brain affect the aggregation of micelles. This knowledge could one day help in the prevention of the onset of Alzheimer’s disease.
Citation
Bryson, A. (2016). Micellular Electrokinetic Chromatography for Studying Amyloid Beta Oligomer Membrane Affinity. Biomedical Engineering Undergraduate Honors Theses Retrieved from https://scholarworks.uark.edu/bmeguht/34
Included in
Amino Acids, Peptides, and Proteins Commons, Bioelectrical and Neuroengineering Commons, Lipids Commons, Medical Neurobiology Commons, Medical Toxicology Commons, Membrane Science Commons, Nervous System Diseases Commons, Neurology Commons