Proteins are the workhorses of human biology. Integrity of protein structures is essential to protein’s physiobiological functions. Protein misfolding is increasingly recognized as an underlying cause of many chronic degenerative diseases, and may have two major consequences: 1) loss of biological function; 2) gain of toxicity or toxic function.

Protein homeostasis (proteostasis) is influenced by the energetics of protein folding, misfolding, and aggregation. Proteostasis is also affected by numerous regulated networks of interacting and competing biological pathways that control the biogenesis, folding, trafficking, and degradation of proteins present within and outside of the cells.

Protego’s technology tackles the protein misfolding problem through modulation of the energetics of protein or protein complexes by binding to small molecules such as pharmacological chaperones and/or by modulation of the cellular folding, secretory, and stress pathways. Protego’s approach builds on the proven pharmacological chaperones approach previously exemplified by tafamidis, discovered and developed by our cofounders Dr. Jeffery W. Kelly and Dr. Richard Labaudinière, for the treatment of transthyretin amyloidosis. The company also builds on the concept of correcting pathologic imbalances in protein homeostasis by specifically activating the unfolded protein response (UPR) with small molecules, to increase cellular folding capacity.