Proteinase inhibition using small Bowman-Birk-type structures

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dc.contributor.authorFernandez, J. H.
dc.contributor.authorMello, M. O.
dc.contributor.authorGalgaro, L.
dc.contributor.authorTanaka, Aparecida Sadae [UNIFESP]
dc.contributor.authorSilva-Filho, M. C.
dc.contributor.authorNeshich, G.
dc.contributor.institutionEmpresa Brasileira de Pesquisa Agropecuária (EMBRAPA)
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionEscuela Super Agr Luiz de Queiroz
dc.contributor.institutionLNCC
dc.date.accessioned2018-06-15T17:30:20Z
dc.date.available2018-06-15T17:30:20Z
dc.date.issued2007-01-01
dc.description.abstractBowman-Birk inhibitors (BBIs) are cysteine-rich and highly cross-linked small proteins that function as specific pseudosubstrates for digestive proteinases. They typically display a double-headed structure containing an independent proteinase-binding loop that can bind and inhibit trypsin, chymotrypsin and elastase. In the present study, we used computational biology to study the structural characteristics and dynamics of the inhibition mechanism of the small BBI loop expressing a 35-amino acid polypeptide (ChyTB2 inhibitor) which has coding region for the mutated chymotrypsin-inhibitory site of the soybean BBI. We found that in the BBI-trypsin inhibition complex, the most important interactions are salt bridges and hydrogen bonds, whereas in the BBI-chymotrypsin inhibition complex, the most important interactions are hydrophobic. At the same time, ChyTB2 mutant structure maintained the individual functional domain structure and excellent binding/ inhibiting capacities for trypsin and chymotrypsin at the same time. These results were confirmed by enzyme-linked immunosorbend assay experiments. The results showed that modeling combined with molecular dynamics is an efficient method to describe, predict and then obtain new proteinase inhibitors. For such study, however, it is necessary to start from the sequence and structure of the mutant interacting relatively strongly with both trypsin and chymotrypsin for designing the small BBI-type inhibitor against proteinases.en
dc.description.affiliationEMBRAPA, Lab Bioinformat Estruct, Campinas, SP, Brazil
dc.description.affiliationUniv Fed Sao Paulo, Escola Paulista Med, Dept Bioquim, Sao Paulo, Brazil
dc.description.affiliationEscuela Super Agr Luiz de Queiroz, Dept Genet, Piracicaba, SP, Brazil
dc.description.affiliationLNCC, LabInfo, Petropolis, RJ, Brazil
dc.description.affiliationUnifespUniv Fed Sao Paulo, Escola Paulista Med, Dept Bioquim, Sao Paulo, Brazil
dc.description.sourceWeb of Science
dc.format.extent846-858
dc.identifierhttp://www.funpecrp.com.br/gmr/year2007/vol4-6/xm0007_abstract.html
dc.identifier.citationGenetics And Molecular Research. Ribeirao Preto: Funpec-editora, v. 6, n. 4, p. 846-858, 2007.
dc.identifier.fileWOS000251697000008.pdf
dc.identifier.issn1676-5680
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/43720
dc.identifier.wosWOS:000251697000008
dc.language.isoeng
dc.publisherFunpec-editora
dc.relation.ispartofGenetics And Molecular Research
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectBowman-Birk inhibitoren
dc.subjectmolecular modelingen
dc.subjectenzyme-linked immunosorbent assayen
dc.subjectenzyme specificityen
dc.titleProteinase inhibition using small Bowman-Birk-type structuresen
dc.typeinfo:eu-repo/semantics/article
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