Structural modelling and thermostability of a serine protease inhibitor belonging to the Kunitz-BPTI family from the Rhipicephalus microplus tick

rBmTI-A is a recombinant serine protease inhibitor that belongs to the Kunitz-BPTI family and was cloned from Rhipicephalus microplus tick. has inhibitory activities on bovine trypsin, human plasma kallikrein, neutrophil elastase plasmin with dissociation constants in nM range. It characterized by two domains each domain presents six cysteines form three disulfide bonds, which contribute high stability of its structure. Previous studies suggest protective potential against pulmonary emphysema mice anti-inflammatory potential. Besides that, presented potent activity vitro vessel formation. In this study, tertiary structure modeled. The stabilization evaluated molecular dynamics analysis. Circular dichroism spectroscopy data corroborated secondary found homology modelling. Also, circular it shown thermostability until approximately 70 °C, assays toward trypsin. • family. (a protein) inhibit Neutrophil Elastase, Kallikreins. A reliable model for obtained Inhibition thermostable up at least °C. Dichroism Spectroscopy corroborate rBmTI-A.