A Molecular Mechanism for Action of Immunophilins and a Method to Identify Novel Pharmaceuticals

The immunophilins are a family of proteins that are functionally related by their rotamase activity (ie they are peptidylprolyl isomerases, PPIase) and their ability to bind immunosuppressive drugs such as FK-506, rapamycin, and cyclosporin A. Immunophilin ligands also hold great promise for the treatment of nerve injuries and neurological diseases. While their mechanism of immunosuppressive activity is understood, the mechanism by which PPIase antagonists exert their neuroprotective activities has been obscure. Investigators at Johns Hopkins recently made a tremendous advance toward an understanding of the mechanism by which PPIase ligands mediate neuroprotection and the induction of neurite outgrowth. These scientists found that PPIase ligands bind to yet another adapter protein that competes with PPIases for binding to proline rich sequences and alters the assembly of signaling complexes. Description (Set) Proposed Use (Set) With an understanding of the molecular basis for the neuroprotective activity of PPIase agents, simple assays can now be established to screen for novel and more effective PPIase antagonists with optimal therapeutic activites. Additionally, these findings validate this adapter protein as an independent target for the development of drugs with an anticipated market that parallels and extends that of PPIase inhibitors.

Inventor(s): Worley, Paul F.

Type of Offer: Licensing

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