Novel Method for Identifying Compounds for Treating Obesity and Neurological Disorders
Vladlen Slepak, Simone Sandiford and Qiang Wang
Problem
Obesity is a health problem affecting approximately 1/3rd of the US population, and the number of new cases is expected to increase in the US, as well as worldwide. Treatment of obesity is currently via a variety of means, but depending on the patient, can cause detrimental side effects and not be effective.
Solution
The importance of Gﾲ5 neuronal protein complex in affecting weight gain has been newly reported, and a specific FRET-based detection method for determining the conformational changes in this complex has been developed. This assay could be used as a screen for therapeutic compounds, and together with a novel mouse model, be key research tools for drug discovery important in weight regulation and some neurological disorders.
Competitive Advantage
A new drug target site for treating obesity and neurological diseases has been identified, and a more specific method than the current biochemical assays for identifying conformational changes at the target site has been developed. By this method, the conformational change and active state of the molecule in real time can be determined, and also in a single cell, allowing for localization.
Applications
The assay and mouse model can be used to identify and test new compounds for obesity and neurological disorder treatments.
Patent Status
US Patent Application based on PCT/US2008/000819 was filed 23 July 2009 and WO 2008/091598 was published 31 July 2008.
Licensing Opportunity
We are seeking commercialization partnerships for a novel approach to treat obesity and neurological diseases.
About the Inventors
Vladlen Slepak, Ph.D., is a Professor in the Department of Molecular and Cellular Pharmacology at the University of Miami Leonard M. Miller School of Medicine.
Ms. Qiang Wang, is a Research Associate in the Department of Microbiology and Immunology.
Ms. Simone Sandiford is pursuing her Ph.D. degree, with Dr. Slepak as her advisor.
Selected References
Narayanan V, Sandiford SL, Wang Q, Keren-Raifman T, Levay K, and Slepak VZ. Intramolecular interaction between the DEP domain of RGS7 and the Gﾲ5 subunit. Biochemistry. 2007, 46:6859-6870.
Sandiford SL and Slepak VZ. Gﾲ5-RGS7 selectively inhibits muscarinic M3 receptor signaling via the interaction between the third intracellular loop of the receptor and the DEP domain of RGS7. Biochemistry. 2009, 48:2282-2289.
