Characterization and pharmacological properties of a novel multifunctional kunitz inhibitor from erythrina velutina seeds

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dc.contributor.authorMorais, Ana Heloneida de Araújo
dc.contributor.authorMachado, Richele Janaína Araújo
dc.contributor.authorMonteiro, Norberto de Kássio Vieira
dc.contributor.authorMigliolo, Ludovico
dc.contributor.authorSilva, Osmar Nascimento
dc.contributor.authorPinto, Michele Flaviane Soares
dc.contributor.authorOliveira, Adeliana
dc.contributor.authorFranco, Octávio Luiz
dc.contributor.authorKiyota, Sumika
dc.contributor.authorBemquerer, Marcelo Porto
dc.contributor.authorUchôa, Adriana Ferreira
dc.contributor.authorSantos, Elizeu Antunes dos
dc.date.accessioned2024-04-12T21:20:55Z
dc.date.available2024-04-12T21:20:55Z
dc.date.issued2013-05
dc.description.resumoInhibitors of peptidases isolated from leguminous seeds have been studied for their pharmacological properties. The present study focused on purification, biochemical characterization and anti-inflammatory and anticoagulant evaluation of a novel Kunitz trypsin inhibitor from Erythrina velutina seeds (EvTI). Trypsin inhibitors were purified by ammonium sulfate (30–60%), fractionation followed by Trypsin-Sepharose affinity chromatography and reversed-phase high performance liquid chromatography. The purified inhibitor showed molecular mass of 19,210.48 Da. Furthermore, a second isoform with 19,228.16 Da was also observed. The inhibitor that showed highest trypsin specificity and enhanced recovery yield was named EvTI (P2) and was selected for further analysis. The EvTI peptide fragments, generated by trypsin and pepsin digestion, were further analyzed by MALDI-ToF-ToF mass spectrometry, allowing a partial primary structure elucidation. EvTI exhibited inhibitory activity against trypsin with IC50 of 2.261028 mol.L21 and constant inhibition (Ki) of 1.061028 mol.L21 , by a non-competitive mechanism. In addition to inhibit the activity of trypsin, EvTI also inhibited factor Xa and neutrophil elastase, but do not inhibit thrombin, chymotrypsin or peptidase 3. EvTI was investigated for its anti-inflammatory and anticoagulant properties. Firstly, EvTI showed no cytotoxic effect on human peripheral blood cells. Nevertheless, the inhibitor was able to prolong the clotting time in a dose-dependent manner by using in vitro and in vivo models. Due to antiinflammatory and anticoagulant EvTI properties, two sepsis models were here challenged. EvTI inhibited leukocyte migration and specifically acted by inhibiting TNF-a release and stimulating IFN-a and IL-12 synthesis. The data presented clearly contribute to a better understanding of the use of Kunitz inhibitors in sepsis as a bioactive agent capable of interfering in blood coagulation and inflammationpt_BR
dc.identifier.citationMACHADO, Richele Janaína Araújo; MONTEIRO, Norberto de Kássio Vieira; MIGLIOLO, Ludovico; SILVA, Osmar Nascimento; PINTO, Michele Flaviane Soares; OLIVEIRA, Adeliana; FRANCO, Octávio Luiz; KIYOTA, Sumika; BEMQUERER, Marcelo Porto; UCHÔA, Adriana Ferreira; MORAIS, Ana Heloneida de Araújo; SANTOS, Elizeu Antunes dos. Characterization and pharmacological properties of a novel multifunctional kunitz inhibitor from erythrina velutina seeds. PloS One, [S.l.], v. 8, n. 5, p. 1-14, 28 mai. 2013. DOI: 10.1371/journal.pone.0063571. Disponível em: https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0063571. Acesso em: 11 abr. 2024.pt_BR
dc.identifier.doihttp://dx.doi.org/10.1371/journal.pone.0063571
dc.identifier.urihttps://repositorio.ufrn.br/handle/123456789/58137
dc.languagept_BRpt_BR
dc.publisherPloS Onept_BR
dc.rightsAttribution 3.0 Brazil*
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/br/*
dc.subjectErythrina velutinapt_BR
dc.subjectMultifunctional propertiespt_BR
dc.subjectAnti-inflammatorypt_BR
dc.subjectTrypsin Inhibitionpt_BR
dc.titleCharacterization and pharmacological properties of a novel multifunctional kunitz inhibitor from erythrina velutina seedspt_BR
dc.typearticlept_BR

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