Abstract
dc:description.abstract<p>Dopamine receptors D1R and D2R form a heterooligomeric complex with signaling properties distinct from the individual receptors. Aberrant expression of this protein-protein complex is linked to the etiology of various neuropsychiatric diseases. Formation of the D1R-D2R heteromer is thought to be dependent upon electrostatic interactions occurring between the carboxyl tail of D1R and the third intracellular loop of D2R. Using this interaction site as template, I synthesized several peptides designed to disrupt the minimal area of the D1R-D2R interaction interface and tested these using whole cell lysates of human brain tissue and dopamine receptor constructs. I report that a synthetic peptide with the sequence EAARRAQE is efficient in blocking D1R-D2R interaction, while shorter and more highly charged peptides (EERRAQ, ARRA and AARRAQ) had no effect. This research provides insight into the binding regions involved in D1-D2 heteromer formation, and may aid future drug development efforts that target this receptor complex.</p>
Degree
thesis:*- Name thesis:degree_name
- Master of Science (MS)
- Level thesis:degree_level
- Open Access Thesis
- Discipline thesis:degree_discipline
- Chemistry
- Year dc:date.available
- 2019
Author and committee
dc:creator, dc:contributor.*- Author dc:creator
-
- Champion, Margaret M.
- Contributors dc:contributor
-
- Hedeel Evans, PhD
- Deborah Heyl-Clegg, PhD
- Jeffery Guthrie, PhD
Subjects
dc:subject × 4Identifiers
dc:identifier.*- Repository record dc:identifier
- https://commons.emich.edu/theses/988
- OAI identifier oai:identifier
- oai:commons.emich.edu:theses-2351