New Compounds For The Treatment Of Diseases Related To Protein Misfolding
- Technology Benefits
- Applicable to broad range of protein misfolding diseasesPrevents formation of new aggregatesBreaks pre-formed aggregates
- Technology Application
- Therapeutic in Alzheimer’s diseaseTherapeutic in Parkinson’s diseaseTherapeutic for protein misfolding disease
- Detailed Technology Description
- UCLA researchers have developed novel compounds based on the β-sheet rich structure adopted by the proteins in the aggregated state. The small molecules bind the β-sheet structure and suppress their formation. They also disassemble pre-formed aggregates robustly. The small molecules have shown to be neuro-protective against amyloid-β induced aggregation and toxicity in cultured cells.
- Others
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Background
Protein misfolding is the underlying cause of a number of neurodegenerative diseases such as Alzheimer’s disease (AD) and Parkinson’s disease (PD) as well systemic diseases such as Type-2 diabetes and prion diseases. In each of these diseases, a protein adopts an altered conformation composed of β-sheets and is found in large deposits that are toxic to cells. For example, AD patients are known to have large β-sheet rich deposits composed of the protein, amyloid-β. Currently, these diseases have no therapeutics and with a global aging population present a huge financial burden.
Related Materials
Additional Technologies by these Inventors
- Small Molecule "Molecular Tweezers" that Inhibit Amyloid-β Fiber Formation
- Preventing Synuclein Accumulation as a Strategy for Improving Neuronal Survival and Regeneration after Spinal Cord Injury
- Inhibition Of Lipofuscin Aggregation By Molecular Tweezers
Tech ID/UC Case
27261/2012-615-0
Related Cases
2012-615-0
- *Abstract
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UCLA researchers in the Department of Neurology with an international team of scientists have developed compounds for therapeutic use in protein misfolding diseases.
- *Principal Investigator
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Name: Gal Bitan
Department:
Name: Sharmistha Sinha
Department:
Name: Katrin Hochdorffer
Department:
Name: Julia Marz-Berberich
Department:
Name: Luitgard Nagel-Steger
Department:
Name: Thomas Schrader
Department:
- Country/Region
- USA
