KLKb2 Inhibitors

Chemical inhibitors of KLKb2 include a variety of compounds that impede the protein's function through different mechanisms of action. Aprotinin acts by forming a complex with the protease domain of KLKb2, thereby obstructing the active site and preventing it from engaging with peptide substrates. Similarly, Benzamidine competes with natural substrates for binding to the active site of KLKb2, achieving inhibition by mimicking substrate structure. AEBSF inhibits KLKb2 irreversibly by covalently attaching to the serine residue within the active site, which is crucial for the enzyme's proteolytic activity. Leupeptin, on the other hand, reversibly binds to the active site and blocks the hydrolysis of peptide bonds, thus inhibiting KLKb2 activity.

Gabexate and Camostat both mimic the transition state of peptide bond hydrolysis to occupy the active site of KLKb2, resulting in the prevention of the protein's interaction with its substrates and subsequent inhibition of its function. Nafamostat also binds to the active site in a similar fashion to Camostat, preventing substrate cleavage and subsequently inhibiting the enzymatic activity of KLKb2. Chymostatin operates by occupying the active site to prevent the proteolytic activity of KLKb2. Soybean trypsin inhibitor (SBTI) directly targets KLKb2 by binding to its active site, inhibiting the enzyme's ability to process substrates. E-64, although typically inhibiting cysteine proteases, can inhibit KLKb2 by irreversibly binding to its active site due to the broad specificity of the protease, leading to inhibited catalytic function. Pepstatin A, which is generally an aspartic protease inhibitor, can inhibit KLKb2 by binding to its active site. Finally, Phosphoramidon may inhibit KLKb2 by chelating metal ions essential for the structural integrity of the protease or for substrate binding, thereby inhibiting the proteolytic function of the protein. Each of these chemicals targets the proteolytic activity of KLKb2 through specific interactions with the active site or essential structural components of the enzyme, leading to functional inhibition.