Inhibition of bovine β-trypsin, human α-thrombin and porcine pancreatic β-kallikrein-B by benzamidine and its bis-, tris- and tetra-derivatives: Thermodynamic and molecular modeling study

Abstract

The inhibitory effect of bis-, tris- and tetra-benzamidine derivatives (DAPP, TAPB and TAPP, respectively) on the catalytic properties of bovine β-trypsin (β-trypsin), human α-thrombin (α-thrombin) and porcine pancreatic β-kallikrein-B (β-kallikrein-B) was investigated (between pH 2.0 and 7.0, I= 0.1 M; T= 37.0 ± 0.5°C), and analyzed in parallel with that of benzamidine, commonly taken as a molecular inhibitor model of serine proteinases