Understanding the molecular basis of devastating diseases caused by misfolded proteins.
Protein misfolding can contribute to disease by disrupting normal protein behavior and generating harmful species. We are developing small molecules designed to stabilize target proteins and interrupt disease processes associated with misfolding.
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.
We develop pharmacological chaperones designed to bind target proteins and stabilize their native fold, with the aim of reducing misfolding and the formation of harmful species.
Our lead program focuses on AL amyloidosis. We are investigating whether stabilizing lambda light chains can address light chain toxicity and contribute to the goal of preserving organ function.
Explore investigational PROT-001 →PROT-001 is investigational. Its safety and efficacy in patients with AL amyloidosis have not been established.