Author

Adam Baraka

Date Approved

2017

Degree Type

Open Access Senior Honors Thesis

Department

Chemistry

First Advisor

Dr. Hedeel Guy Evans

Second Advisor

Dr. Deborah Heyl-Clegg

Abstract

The dopamine receptor subtypes known as DI and D2 have been shown to form a heteromer complex, which is thought to lead to the disruption of a multitude of signaling pathways within the brain. As a result, this has been proposed to lead to diseased states such as Alzheimer's and depression. In previous studies, it has been shown that the use of synthetic peptides corresponding to the surface interface of the interactions (specifically in the third intracellular loop of D2 interface) within the complex have served to compete against the formation of the heteromer. Through in vitro biochemical techniques such as SDS-Page and Western blotting, we observed the degree of dissociation of the Dl-D2 complex through a variety of small peptides. These peptides consist of peptide 1, 2, 3 and 4 with the sequences corresponding to Ac-EAARRAQE, AcEERRAQ, Ac-ARRA, and Ac-AARRAQ, respectively. Peptide 1 was found to be the most effective in preventing complex formation.

Included in

Chemistry Commons

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