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Novel Therapeutics for Disease Associated with Protein Misfolding and Aggregation

Researchers at the University of Missouri (MU) have designed novel cell-penetrating minichaperones (CPMC’s) that have been demonstrated in vitro and in vivo to 1) suppress protein aggregation, 2) increase resistance to heat shock, 3) reduce apoptosis, and 4) extend lifespan in C. elegans. These compounds are designed to resist proteolysis, to maintain cellular homeostatis in disease states, and have great potential in treating proteopathies such as Alzheimer’s, Parkinson’s, Creutzfeldt-Jakob, and others.

Appropriate protein folding is critical for proper protein function. Misfolding can cause non-functional protein-protein interactions that result in protein aggregation and decreases in essential cellular functions, homeostasis, translocation, and clearance of other proteins. These defects can lead to variety of diseases that adversely affect human health.

As protein misfolding has dire consequences, nature has designed specialized proteins to assist in appropriate folding. These proteins, known as chaperones hold great potential in treating proteopathic conditions.

Using insight based on decades of research focused on protein misfolding and chaperones, MU researchers have designed novel therapeutics for the treatment of a variety of proteopathies.
- Potential therapeutic for a broad spectrum of proteopathic diseases including Creutzfeldt–Jakob and other prion diseases, Alzheimer's disease, Parkinson's disease, amyloidosis, multiple system atrophy, and a wide range of other disorders

- Resistant to proteolysis
- Cell-penetrating properties
- CMPC’s are nontoxic to other cells

State of Development
In vitro and in vivo data have been generated in cell and animal models

Additional Details


University of Missouri-Columbia

Intellectual Property Protection

Pending Patent

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