Abstract：
:rBmTI-A is a recombinant serine protease inhibitor that belongs to the Kunitz-BPTI family and that was cloned from Rhipicephalus microplus tick. rBmTI-A has inhibitory activities on bovine trypsin, human plasma kallikrein, human neutrophil elastase and plasmin with dissociation constants in nM range. It is characterized by two inhibitory domains and each domain presents six cysteines that form three disulfide bonds, which contribute to the high stability of its structure. Previous studies suggest that serine protease inhibitor rBmTI-A has a protective potential against pulmonary emphysema in mice and anti-inflammatory potential. Besides that, rBmTI-A presented a potent inhibitory activity against in vitro vessel formation. In this study, the tertiary structure of rBmTI-A was modeled. The structure stabilization was evaluated by molecular dynamics analysis. Circular dichroism spectroscopy data corroborated the secondary structure found by the homology modelling. Also, in circular dichroism data it was shown a thermostability of rBmTI-A until approximately 70 °C, corroborated by inhibitory assays toward trypsin.
journal_name
Biochimiejournal_title
Biochimieauthors
Bomediano Camillo LM,Ferreira GC,Duran AFA,da Silva FRS,Garcia W,Scott AL,Sasaki SDdoi
10.1016/j.biochi.2020.12.014subject
Has Abstractpub_date
2020-12-24 00:00:00pages
226-233eissn
0300-9084issn
1638-6183pii
S0300-9084(20)30336-9journal_volume
181pub_type
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