Cathepsins are a family of proteases that have been implicated in many diseases.
Virobay compounds are highly potent, orally active and drug-like; addressing common problems in the design of cathepsin inhibitors.
Proteases catalyze the breakdown of proteins through the hydrolysis of peptide bonds. Genomic analysis has identified more than 500 proteases in the human genome. Their expression and activity is highly regulated and dysregulation of protease function has been implicated in a variety of diseases, such as autoimmune disorders, neuropathic pain, atherosclerosis, liver fibrosis and cancer, making them attractive targets for small molecule drug development.
The cathepsins are a subclass of proteases with both intracellular and extracellular function. The best characterized and largest class of the cathepsins are the cysteine proteases in the papain family namely cathepsins B, C, F, H, L, K, O, S, V, W, and X. Although many cathepsins are active as lysosomal proteases, some cathepsins are important in cytosolic and extracellular functions as well. Activity of specific members of the cathepsin family has been implicated in a number of diseases as indicated above. Virobay is a leader in the design, synthesis and development of small molecule cysteine protease inhibitors for these attractive therapeutic targets.