(198f) Electrophoretic Separation of Amyloid Proteins Via Capillary Electrophoresis

The complete sequencing of the human genome has opened the door for the next phase of research, proteomics. Proteomics is a rapidly expanding field and has practical applications for studies of disease-related proteins, such as amyloid proteins. Amyloid proteins, such as insulin and amyloid β (Aβ), are capable of undergoing self-assembly to form oligomeric species and eventually insoluble aggregates. The formation of these species has been linked to the development of diseases including Diabetes and Alzheimer's Disease (AD). A number of technical challenges exist for the quantitative analysis of the different sizes of amyloid proteins which are present during the early stages of aggregation, therefore requiring new technologies to be developed for enhanced protein separations. Microchannel electrophoretic techniques have emerged as powerful tools for the quantitative analysis of proteins. In addition, diagnostic applications of microchannel techniques for the early detection of Aβ protein may offer a means to diagnose and/or prevent AD. This work utilizes capillary electrophoresis (CE) for studies of the early stages of insulin and Aβ aggregation. Previously, we investigated the ability of CE to monitor insulin oligomerization and aggregation over time and worked to develop a model for calculating species sizes. Further, we determined that FITC-labeled insulin was unable to incorporate into the growing aggregation species. Here we extend our previous work to other amyloid proteins, Aβ 1-40 and 1-42.