N EW TECHNOLOGY DISCLOSURE Amyloid -Protein Aggregation Inhibitors Novel disubstituted peptides disrupt the formation of the amyloid -protein fibrils associated with Alzheimer’s disease, and destabilize already-formed fibrils. Patent Status: Patented Technology Status: Animal studies in progress Terms: Exclusive or Non-Excl. Availability: Immediate Inhibition of amyloid -protein aggregation and dissolution of existing aggregates may provide an effective treatment for Alzheimer’s disease. Principal Investigator Robert P. Hammer Long-standing evidence shows that cerebral deposition of amyloid -protein (A ) fibrils and plaque plays a central role in the progressive neural degeneration of Alzheimer’s William A. Pryor Professor disease. There is therefore great interest in controlling the proteolytic conversion of Dept. of Chemistry amyloid precursor protein (APP) to A , or modulating the Applications [email protected] seemingly irreversible aggregation of A into -pleated sheets that form the damaging fibrils and plaque. Potential treatment for We have developed several amyloid aggregation- Alzheimer’s disease mitigating peptide (AAMP) analogs that display signifi- Potential for other LSU OIP 0212 cantly better in vitro and in vivo interference of A fibril- proteopathies: logenesis than previously existing peptide analogs, and Prion diseases For licensing, contact: that can dissolve already-formed fibrils in vitro. Parkinson’s disease Amyotrophic lateral sclerosis Peter J. Kelleher Our fibril inhibitors are designed to interact with A via Associate Vice-Chancellor hydrogen bonding and side-chain interactions at the fi- Nanotechnology bril’s -pleated sheet edge, preventing further A aggre- Modulation of peptide-based Office of Intellectual Property, gation by blocking the hydrogen bonding that appears to structures Commercialization and Development stabilize fibril formation. We have shown that while pure 206 Louisiana Emerging Technology Center A solutions form fibrils in vitro, our AAMP/A mix- Baton Rouge, LA 70803 tures show no fibrillization or gelation even after months at room temperature. Preliminary animal studies are consistent Phone: 225-615-8967 with these in vitro results. Fax: 225-615-8965 E-mail: [email protected] Our AAMPS are very stable and do not aggregate in solu- RESEARCH & ECONOMIC tion. DEVELOPMENT Non-Confidential Disclosure. © Louisiana State University 2007. All Rights Reserved. .