KLK13 Inhibitors

KLK13 inhibitors encompass a range of chemical structures and mechanisms but ultimately converge on the specific inhibition of KLK13 and its associated pathways. For example, AEBSF and Benzamidine function as direct inhibitors that interact with the active site of the enzyme, it from engaging in proteolytic activity. These agents offer immediate, specific inhibition and have the advantage of blocking KLK13's action without involving other cellular elements. SBTI, Aprotinin, and Nafamostat follow a similar trend by forming inhibitory complexes with KLK13, thereby eliminating its enzymatic action. Indirect inhibitors like Leupeptin, E-64, and EACA manipulate the broader biochemical environment to limit KLK13 activity. Leupeptin inhibits cysteine and serine proteases, resulting in fewer available peptide substrates for KLK13. E-64 limits the supply of such substrates by inhibiting cysteine proteases, and EACA interferes with the plasminogen activation system, affecting the range of substrates that KLK13 can act upon. These inhibitors modify the substrate landscape or adjust the biochemical parameters under which KLK13 operates, offering different strategic options for regulating this enzyme.