Interaction between insulin receptor and a peptide derived from a trypsin inhibitor purified from tamarind seed: An in silico screening of insulin-like peptides

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dc.contributor.authorVale, Sancha Helena de Lima
dc.contributor.authorGomes, Ana Francisca Teixeira
dc.contributor.authorMedeiros, Wendjilla Fortunato de
dc.contributor.authorBezerra, Lucas Lima
dc.contributor.authorLuz, Anna Beatriz Santana
dc.contributor.authorSousa Junior, Francisco Canindé de
dc.contributor.authorSantos, Eliseu Antunes dos
dc.contributor.authorMonteiro, Norberto de Kássio Vieira
dc.contributor.authorMorais, Ana Heloneida de Araújo
dc.contributor.authorIDhttps://orcid.org/0000-0002-0972-1678
dc.contributor.authorIDhttps://orcid.org/0000-0002-5565-7101
dc.contributor.authorIDhttps://orcid.org/0000-0003-2042-4348
dc.contributor.authorIDhttps://orcid.org/0000-0002-6460-911X
dc.date.accessioned2025-06-18T23:04:37Z
dc.date.available2025-06-18T23:04:37Z
dc.date.issued2024-06
dc.description.resumoThe aim of this study was to prospect in silico peptides derived from a multifunctional protein and assess their interaction with the insulin receptor (IR). The trypsin inhibitor isolated from tamarind seeds (TTI) was obtained through trypsin sepharose 4B-CNBr affinity chromatography and subsequently characterized. The TTI underwent in vitro hydrolysis to assess its susceptibility to enzymatic degradation and determine suitable enzymes for cleavage in silico. The theoretical model was established to assess the purified tamarind seed trypsin inhibitor (TTIp 56/287) being cleaved in silico and selected for simulation by molecular dynamics. Among the peptides generated, Peptidetripquimo59 presented the most negative docking score (-175.53) with the IR, indicating strong affinity and stability in complex formation. Significant interaction with the IR was observed for key residues, including arginine 16 (-209.07 kJ mol-1), threonine 1 (-148.54 kJ mol-1), and valine 2 (-94.53 kJ mol1). Additionally, it was discovered that both insulin and Peptidetripquimo59 exhibit binding to the identical location on the insulin receptor (IR). The results of the semi-empirical approach revealed that Peptidetripquimo59 exhibited greater potential for interaction with the IR compared to other complexes such as the insulin-IR complex, suggesting its candidacy as a starting point for the development of therapeutic agents targeting both type 1 and type 2 Diabetes mellitus
dc.identifier.citationGOMES, Ana Francisca Teixeira; MEDEIROS, Wendjilla Fortunato de; BEZERRA, Lucas Lima; LUZ, Anna Beatriz Santana; SOUSA JUNIOR, Francisco Canindé de; VALE, Sancha Helena de Lima; SANTOS, Elizeu Antunes dos; MONTEIRO, Norberto de Kássio Vieira; MORAIS, Ana Heloneida de Araújo. Interaction between insulin receptor and a peptide derived from a trypsin inhibitor purified from tamarind seed: an in silico screening of insulin-like peptides. Arabian Journal of Chemistry, [S.l.], v. 17, n. 6, p. 1-15, jun. 2024. DOI: 10.1016/j.arabjc.2024.105780. Disponível em: https://www.sciencedirect.com/science/article/pii/S1878535224001825?via%3Dihub. Acesso em: 12 jul. 2024.
dc.identifier.urihttps://doi.org/10.1016/j.arabjc.2024.105780
dc.identifier.urihttps://repositorio.ufrn.br/handle/123456789/64012
dc.language.isoen_US
dc.publisherArabian Journal of Chemistry
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Brazilen
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/br/
dc.subjectComputer Simulation
dc.subjectPeptides
dc.subjectDiabetes Mellitus
dc.subjectHypoglycemic Agents
dc.subjectTherapeutics
dc.titleInteraction between insulin receptor and a peptide derived from a trypsin inhibitor purified from tamarind seed: An in silico screening of insulin-like peptides
dc.typearticle

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