Date of Award
2016
Document Type
Dissertation/Thesis
Submission Date
October 2026
Thesis/Dissertation Advisor [Chair]
Bohn, Laura
Thesis/Dissertation Co-Chair
Schmid, Cullen
Abstract
Opioids are considered the most efficacious drugs for management of moderate to severe pain, yet their use clinically is often restricted due to the onset of adverse side-effects. Drugs in this class produce most of their physiological effects (analgesia, nausea, vomiting) through activation of the μ-opioid receptor; however, an increasing number of studies have demonstrated that opioids can activate distinct downstream responses, a phenomenon termed functional selectivity. This project attempts to determine the amino acid residues involved in the activation of the μ-opioid receptor and the role they play in the binding of ligands to the receptor. The highly conserved DRY motif (aspartic acid-arginine-tyrosine) found commonly in GPCRs was mutated via site directed mutagenesis, aspartic acid-164 to alanine (A), glutamic acid (E), and arginine (R) and G-protein coupling and competition binding assays were performed to test whether ligand affinity and activity differed in the mutant receptors compared to the wild-type.
Recommended Citation
Zimmerman, Frank, "Evaluating the DRY motif and its effects on ligand binding at the µ-Opioid Receptor" (2016). Harriet L Wilkes Honors College Theses 2010 - 2019. 254.
https://digitalcommons.fau.edu/etd_honors_2/254
Extent
31 p.
Identifier
FA00003698
Comments
Includes bibliography.