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Kallikrein inhibitors block plasma and tissue kallikreins, serine proteases that release kinin peptides. Plasma kallikrein circulates as an inactive precursor and is activated together with coagulation factor XII during contact activation. The active enzyme cleaves high-molecular-weight kininogen to release bradykinin, a peptide that raises vascular permeability. Tissue kallikrein and the kallikrein-related peptidases (KLK1 to KLK15) form a separate family of secreted proteases studied in skin biology and cancer. Sebetralstat and berotralstat inhibit plasma kallikrein, while Kallikrein 5-IN-2 acts on KLK5 and FE-999024 on tissue kallikrein. D-Pro-Phe-Arg-Chloromethylketone blocks both factor XII and kallikrein, the two proteases that start contact activation. The chromogenic substrate D-Val-Leu-Arg-pNA acetate is used to measure kallikrein activity in enzyme assays.
KLK7 modulator-1 is a modulator that targets the kallikrein-related peptidase 7 (KLK7). This compound has been shown to influence KLK7 activity, which is implicated in various biological processes, including skin homeostasis and cancer progression. Research applications include studies on protease regulation and the role of KLK7 in disease mechanisms.
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