Understanding the molecular basis of devastating diseases caused by misfolded proteins.
Protein misfolding drives many serious diseases. When proteins lose their native structure, they can lose function and form toxic aggregates that disrupt cells and tissues. For most of these conditions, treatment options remain limited or nonexistent because traditional approaches do not address the underlying structural defect. We are advancing targeted conformational stabilization to stop disease at its molecular source.
Proteins must fold into precise three-dimensional structures to function properly. Genetic mutations, cellular stress, and aging can cause them to misfold, leading to loss of function, toxic aggregation, and disease.
Our platform discovers high-affinity pharmacological chaperones that bind and stabilize proteins in their native fold, preventing the cascade of proteotoxic events that follows misfolding.
By restoring conformational stability, our therapies have the potential to halt disease progression and preserve normal protein function—offering new hope to patients with few or no treatment options today.