Date of Award

5-2013

Degree Type

Honors College Thesis

Department

Chemistry and Biochemistry

First Advisor

Vijay Rangachari, Ph.D.

Advisor Department

Chemistry and Biochemistry

Abstract

Alzheimer’s disease (AD) is a neurodegenerative disorder characterized by cognitive dysfunction and memory loss, and pathologically characterized by amyloid-beta (Aβ) plaques and inflammation. Recent research has shown that these Aβ plaques are also found in traumatic

brain injury (TBI) patients. This discovery has led to a proposed pathway leading from traumatic brain injuries to dementia, more specifically AD. After a TBI, human granulin-A (GRN) and interleukin-8 (IL8) are released and the number of elastases in the brain increases in response to the inflammation response. IL8 is a cytokine that is released in acute inflammation responses, and the levels of IL8 secreted are increased. Because of the presence of Aβ plaques in the brains of TBI patients soon after the initial injury, it can be hypothesized that IL8 plays a role in the aggregation of these Aβ plaques because of the inflammation response associated with this cytokine, as well as the increased presence of IL8 in the brain. In order to examine the possible interactions between IL8 and Aβ, the protein IL8 is being recombinantly expressed in E. coli, and then purified using a nickel column. After purification, the protein will be characterized using circular dichroism (CD), Ellman’s Assay, and mass spectrometry. The interactions between IL8 and Aβ are being examine using ThioflavinT (ThT) fluorescence and SDS-PAGE. When the results of the purification are examined, they show that the protein obtained was pure and in the correct conformation. The interaction studies using ThT showed inhibition of Aβ aggregation in the presence of IL8. Overall, the results from the research indicate that IL8 does play an inhibitory role in the aggregation of Aβ.

Included in

Life Sciences Commons

Share

COinS