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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

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Author(s):
Bomediano Camillo, Livia de Moraes [1] ; Ferreira, Graziele Cristina [1] ; Alves Duran, Adriana Feliciano [1] ; Santos da Silva, Flavia Ribeiro [1] ; Garcia, Wanius [2] ; Scott, Ana Ligia [3] ; Sasaki, Sergio Daishi [1]
Total Authors: 7
Affiliation:
[1] Univ Fed ABC, Ctr Ciencias Nat & Humanas, Sao Bernardo Do Campo, SP - Brazil
[2] Univ Fed ABC, Ctr Ciencias Nat & Humanas, Santo Andre, SP - Brazil
[3] Univ Fed ABC, Ctr Matemat Comp & Cognicao, Santo Andre, SP - Brazil
Total Affiliations: 3
Document type: Journal article
Source: Biochimie; v. 181, p. 226-233, FEB 2021.
Web of Science Citations: 0
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 degrees C, corroborated by inhibitory assays toward trypsin. (C) 2020 Elsevier B.V. and Societe Francaise de Biochimie et Biologie Moleculaire (SFBBM). All rights reserved. (AU)

FAPESP's process: 11/07001-7 - Studies of effect of serineproteinase inhibitors from Rhipicephalus Boophilus microplus tick into lung emphysema induced in mice and molecular characterization of serineproteinases activities present in its experimental model
Grantee:Sergio Daishi Sasaki
Support type: Regular Research Grants
FAPESP's process: 17/19077-4 - Structural dynamics and molecular mechanisms involved in the alpha-synuclein aggregation
Grantee:Ana Ligia Scott
Support type: Scholarships abroad - Research
FAPESP's process: 18/11874-5 - Serine proteinase inhibitors in pulmonary cells and in emphysema
Grantee:Sergio Daishi Sasaki
Support type: Regular Research Grants
FAPESP's process: 17/17275-3 - Studies of the mode of action of two lytic polysaccharide monooxygenases from insect (order: isoptera): molecular structure, bioinorganic chemistry and biotechnological applications
Grantee:Wanius José Garcia da Silva
Support type: Regular Research Grants