The study of the formation of oligomers and amyloid plaques from Amylin by capillary electrophoresis and fluorescent microchip electrophoresis

Amylin, a pancreatic β-cell hormone, was the focus of this research project. This hormone is co-localized and co-secreted with insulin in response to nutrient stimuli. The hormone inhibits food intake, gastric emptying and glucagon secretion. Insulin and amylin appear to complement each other in the control of plasma glucose levels. Human amylin has a propensity to self-aggregate and to form insoluble bodies. In type 2 diabetes, amylin forms pancreatic islet amyloid plaques, which are found in 90% of people with the disease. It is still uncertain whether or not the deposition of amylin is a primary, or a secondary, event in the development of type 2 diabetes. Oligomers of amylin have been recently suggested as the cytotoxic cause of cell death; this is in opposition to larger amyloid deposits being the cause of β-cell deaths. This project examined the aggregation of Amylin. By using capillary electrophoresis and microchip electrophoresis we attempted to determine the earliest time points of amylin oligomer formation and monitor them as they continue to increase in size. The successful development of this method could allow researchers to better understand the cytotoxicity of amylin oligomers and in turn lead to better treatments and potentially earlier diagnosis for type 2 diabetes patients. Our current research was able to see Amylin aggregation with capillary electrophoresis, however the optimized conditions to best characterize the Amylin aggregates still needs to be determined. The microchip studies were not pursued far enough to observe Amylin aggregates through that process.