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.

Background

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.

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.

Background

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.

Additional Details