The Biocompare Inhibitor Search Tool lets researchers browse thousands of compounds by searching by inhibitor name or by its target enzyme. Enter the inhibitor name under "Keywords" or enter the target protein name under "Inhibitor Target.” You may also check the appropriate boxes to further narrow your search.
Cysteine protease inhibitors are compounds that block or inhibit the bioactivity of peptidases in the cysteine protease family. This protease classification, defined by a nucleophilic cysteine thiol inside a catalytic triad, includes proteases such as papain, cathepsins, calpain, and TEV protease. Small molecule or peptide inhibitors of cysteine proteases act by binding to the enzyme and preventing catalytic activity directly, or indirectly through a conformational change. E-64, a small molecule, is an irreversible inhibitor of a broad range of cysteine proteases. Others, such as ALLN, is a specific peptide inhibitor of calpains and cathepsins. Visit the inhibitor supplier page for more information, including purity and other technical data.