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Cysteine protease inhibitors block enzymes that cut peptide bonds with a thiol group in the active site. The papain-like cysteine cathepsins work mainly in lysosomes, where they degrade proteins and process antigens and prohormones. Calpains are calcium-dependent cytosolic cysteine proteases that cleave cytoskeletal and signaling proteins at limited sites rather than digesting them completely. Both groups are studied in models of bone resorption, neurodegeneration, muscle wasting and tumor invasion. CA-074 inhibits cathepsin B, and CA-074 Methyl Ester is its membrane-permeable ester. Odanacatib targets cathepsin K, the main collagen-degrading protease of osteoclasts. MDL 28170 and PD 150606 inhibit calpains, while aloxistatin acts broadly on cysteine proteases.
Synonyms: H-Gly-Phe-BNA
Gly-Phe-beta-naphthylamide is a cathepsin C substrate. The compound is described to accumulate inside lysosomes leading to their destruction.
