Design and Synthesis of 1,3-Disubstitiuted-2-Pyridones as a New Class of Glycogen Phosphorylase Inhibitors
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Glycogen Phosphorylase (GP) is the regulatory enzyme that catalyses the first step in glycogen degradation and is a potential enzyme target for therapeutic intervention in the treatment of diabetes. The 16 amino acid C-terminal sequence of human Gl is the only known targeting subunit that binds to GPa. Blocking the interactions between Gl and GPa should reduce high blood glucose levels in a diabetic person. A segment of the 16 amino acid segment was chosen for a small molecule peptidomimetric approach, and de nova design from this segment identified the pyridone ring as apotential scaffold. This thesis reports the design and synthesis of 1.3-disubstituted pyridones as new class of GPa inhibitors.
Thesis (PhD Doctorate)
Doctor of Philosophy (PhD)
Eskitis Institute for Cell and Molecular Therapies
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This thesi was scanned. The appendix and published articles have not been published.
Glycogen phosphorylase inhibitors