Date of Graduation

5-2012

Document Type

Thesis

Degree Name

Bachelor of Science in Chemical Engineering

Degree Level

Undergraduate

Department

Chemical Engineering

Advisor/Mentor

Hestekin, Christa N.

Abstract

Alzheimer’s disease (AD) is the leading cause of dementia accounting for ½ to ¾ of all cases. AD is characterized by a progressive loss of cognitive function over a span of 10 years, ultimately ending in death. The main possible cause of AD being researched is the formation of soluble, oligomer amyloids. Amyloids are proteins that misfold and aggregate in the brain causing potent neurotoxic effects on neurons in the brain. Microchip electrophoresis and capillary electrophoresis are two potential methods of determining the level of amyloid aggregation. In order to detect at physiological concentrations, covalent dyes must be used to allow the protein to be visualized. However, covalent dyes have been shown to inhibit. The dyes may be inhibiting aggregation in any of the following ways: the attachment site of the dye to a particular group interfering with key reactions, the aromatic structure of FAM acting as an inhibitor, or the dye attachment altering a necessary charged group. In this study, the model protein albumin was labeled with BODIPY-FL dye and run through a column to separate the labeled protein from the excess dye. However, the albumin and BODIPY would not elute from the column in the original experiment. The albumin and BODIPY were run separately through a much smaller column to test if they were getting stuck in the packing. Based on UV absorbance reading from the column elutions, it was determined that albumin was getting stuck in the column. In order to move forward, a better buffer could be used to push the albumin through the column or a different model protein could be used that didn’t get stuck in the column.

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