Structural insights and molecular dynamics into the inhibitory mechanism of a kunitz-type trypsin inhibitor from tamarindus indica L

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dc.contributor.authorMaciel, Bruna Leal Lima
dc.contributor.authorMedeiros, Amanda Fernandes de
dc.contributor.authorSouza, Beatriz Blenda Pinheiro de
dc.contributor.authorCoutinho, Lucas Pinheiro
dc.contributor.authorMurad, Aline Melro
dc.contributor.authorSantos, Paula Ivani Medeiros dos
dc.contributor.authorMonteiro, Norberto de Kássio Vieira
dc.contributor.authorSantos, Elizeu Antunes dos
dc.contributor.authorMorais, Ana Heloneida de Araújo
dc.date.accessioned2024-01-30T13:35:45Z
dc.date.available2024-01-30T13:35:45Z
dc.date.issued2021-01
dc.description.resumoTrypsin inhibitors from tamarind seed have been studied in vitro and in preclinical studies for the treatment of obesity, its complications and associated comorbidities. It is still necessary to fully understand the structure and behaviour of these molecules. We purifed this inhibitor, sequenced de novo by MALDI-TOF/ TOF, performed its homology modelling, and assessed the interaction with the trypsin enzyme through molecular dynamics (MD) simulation under physiological conditions. We identified additional 75 amino acid residues, reaching approximately 72% of total coverage. The four best conformations of the best homology modelling were submitted to the MD. The conformation n287 was selected considering the RMSD analysis and interaction energy (–301.0128 kcal.mol1 ). Residues Ile (54), Pro (57), Arg (59), Arg (63), and Glu (78) of pTTI presented the highest interactions with trypsin, and arginine residues were mainly involved in its binding mechanism. The results favour bioprospecting of this protein for pharmaceutical health applicationspt_BR
dc.identifier.citationMEDEIROS, Amanda Fernandes de; SOUZA, Beatriz Blenda Pinheiro de; COUTINHO, Lucas Pinheiro; MURAD, Aline Melro; SANTOS, Paula Ivani Medeiros dos; MONTEIRO, Norberto de Kássio Vieira; SANTOS, Elizeu Antunes dos; MACIEL, Bruna Leal Lima; MORAIS, Ana Heloneida de Araújo. Structural insights and molecular dynamics into the inhibitory mechanism of a kunitz-type trypsin inhibitor from tamarindus indica L. Journal Of Enzyme Inhibition And Medicinal Chemistry, [S.l.], v. 36, n. 1, p. 480-490, 24 jan. 2021. DOI: 10.1080/14756366.2021.1876686. Disponível em: https://www.tandfonline.com/doi/full/10.1080/14756366.2021.1876686. Acesso em: 25 jan. 2024.pt_BR
dc.identifier.doihttp://dx.doi.org/10.1080/14756366.2021.1876686
dc.identifier.urihttps://repositorio.ufrn.br/handle/123456789/57449
dc.languageenpt_BR
dc.publisherJournal of Enzyme Inhibition and Medicinal Chemistrypt_BR
dc.rightsAttribution-NonCommercial 3.0 Brazil*
dc.rights.urihttp://creativecommons.org/licenses/by-nc/3.0/br/*
dc.subjectTamarindpt_BR
dc.subjectAntitrypticpt_BR
dc.subjectHomology modellingpt_BR
dc.subjectComputational methodspt_BR
dc.subjectProtein-protein interactionpt_BR
dc.titleStructural insights and molecular dynamics into the inhibitory mechanism of a kunitz-type trypsin inhibitor from tamarindus indica Lpt_BR
dc.typearticlept_BR

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