Class
Article
College
College of Science
Department
Biology Department
Faculty Mentor
Erin Bobeck
Presentation Type
Poster Presentation
Abstract
G protein-coupled receptors (GPCRs) are a relatively new discovery in molecular biology and have been fundamental for the development of new drug therapies. GPCRs are receptors within the outer membrane of a cell that trigger reactions throughout a cell. There are multiple units that attach to the GPCR: the alpha, the beta, and the gamma subunits. A ligand (activating or agonistic molecule) binds to the protein receptor, causing a change in structure that allows the attached subunits to move. These movements can generate various signaling pathways that can change a cell. This experiment focuses on the alpha sub-unit whose movement causes the production of cAMP. Enzyme adenylyl cyclase is responsible for producing cAMP which is vital for many cellular functions, such as gene transcription, metabolism, and muscle contraction. Regulation of cAMP can lead to the inhibition or enhancement of many of these processes following activation of GPCRs. Such regulation already occurs naturally via the alpha subunits, which are highly involved with cAMP production and serve as inhibitory or activating proteins. One such protein is GPR171, which is greatly involved in morphine-induced analgesia (pain-relief). Research from the Bobeck lab has shown that a non-addictive drug that activates GPR171, MS0015203, is capable of enhancing morphine’s pain-relieving properties, making it a potential treatment for chronic pain. Fourteen new drugs, synthesized and designed by our collaborator Dr. Sanjai Kumar Pathak, from Queen’s College in New York, are based on this MS0015203 structure but with slight structural modifications. This research will attempt to determine which of these modifications to MS0015203 will make it more efficient in inhibiting the production of cAMP, which will indicate which modified ligands have the most potential as new pain-therapies.Presentation Time: Wednesday, 3-4 p.m.
Location
Logan, UT
Start Date
4-11-2021 12:00 AM
Included in
Discerning the Efficacy of Potential Non-Opioid Pain Drugs With cAMP Analysis
Logan, UT
G protein-coupled receptors (GPCRs) are a relatively new discovery in molecular biology and have been fundamental for the development of new drug therapies. GPCRs are receptors within the outer membrane of a cell that trigger reactions throughout a cell. There are multiple units that attach to the GPCR: the alpha, the beta, and the gamma subunits. A ligand (activating or agonistic molecule) binds to the protein receptor, causing a change in structure that allows the attached subunits to move. These movements can generate various signaling pathways that can change a cell. This experiment focuses on the alpha sub-unit whose movement causes the production of cAMP. Enzyme adenylyl cyclase is responsible for producing cAMP which is vital for many cellular functions, such as gene transcription, metabolism, and muscle contraction. Regulation of cAMP can lead to the inhibition or enhancement of many of these processes following activation of GPCRs. Such regulation already occurs naturally via the alpha subunits, which are highly involved with cAMP production and serve as inhibitory or activating proteins. One such protein is GPR171, which is greatly involved in morphine-induced analgesia (pain-relief). Research from the Bobeck lab has shown that a non-addictive drug that activates GPR171, MS0015203, is capable of enhancing morphine’s pain-relieving properties, making it a potential treatment for chronic pain. Fourteen new drugs, synthesized and designed by our collaborator Dr. Sanjai Kumar Pathak, from Queen’s College in New York, are based on this MS0015203 structure but with slight structural modifications. This research will attempt to determine which of these modifications to MS0015203 will make it more efficient in inhibiting the production of cAMP, which will indicate which modified ligands have the most potential as new pain-therapies.Presentation Time: Wednesday, 3-4 p.m.