Navegando por Autor "Bezerra, Lucas Lima"
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Artigo An insulin receptor-binding multifunctional protein from tamarindus indica L. presents a hypoglycemic effect in a diet-induced type 2 diabetes-preclinical study(Foods, 2022-07) Maciel, Bruna Leal Lima; Costa, Izael de Sousa; Lima, Mayara Santos Rosa; Medeiros, Amanda; Bezerra, Lucas Lima; Santos, Paula; Serquiz, Alexandre; Lima, Maíra Conceição Jerônimo de Souza; Oliveira, Gerciane Santos de; Santos, Elizeu Antunes dos; Monteiro, Norberto de Kássio Vieira; Morais, Ana HeloneidaThe objectives of this study were to evaluate the hypoglycemic effect of the trypsin inhibitor isolated from tamarind seeds (TTI) in an experimental model of T2DM and the in silico interaction between the conformational models of TTI 56/287 and the insulin receptor (IR). After inducing T2DM, 15 male Wistar rats were randomly allocated in three groups (n = 5): 1—T2DM group without treatment; 2—T2DM group treated with adequate diet; and 3—T2DM treated with TTI (25 mg/kg), for 10 days. Insulinemia and fasting glucose were analyzed, and the HOMA-IR and HOMA-β were calculated. The group of animals treated with TTI presented both lower fasting glucose concentrations (p = 0.0031) and lower HOMA-IR indexes (p = 0.0432), along with higher HOMA-β indexes (p = 0.0052), than the animals in the other groups. The in silico analyses showed that there was an interaction between TTIp 56/287 and IR with interaction potential energy (IPE) of −1591.54 kJ mol−1 (±234.90), being lower than that presented by insulin and IR: −894.98 kJ mol−1 (±32.16). In addition, the presence of amino acids, type of binding and place of interaction other than insulin were identified. This study revealed the hypoglycemic effect of a bioactive molecule of protein origin from Tamarind seeds in a preclinical model of T2DM. Furthermore, the in silico analysis allowed the prediction of its binding in the IR, raising a new perspective for explaining TTI’s action on the glycemic responseArtigo 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, 2024-06) Vale, Sancha Helena de Lima; Gomes, Ana Francisca Teixeira; Medeiros, Wendjilla Fortunato de; Bezerra, Lucas Lima; Luz, Anna Beatriz Santana; Sousa Junior, Francisco Canindé de; Santos, Eliseu Antunes dos; Monteiro, Norberto de Kássio Vieira; Morais, Ana Heloneida de Araújo; https://orcid.org/0000-0002-0972-1678; https://orcid.org/0000-0002-5565-7101; https://orcid.org/0000-0003-2042-4348; https://orcid.org/0000-0002-6460-911XThe 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 mellitusArtigo Prospecting native and analogous peptides with anti-SARS-CoV-2 potential derived from the trypsin inhibitor purified from tamarind seeds(Elsevier, 2023) Morais, Ana Heloneida de Araújo; Luz, Anna Beatriz Santana; Medeiros, Amanda Fernandes de; Bezerra, Lucas Lima; Lima, Mayara Santa Rosa; Pereira, Annemberg Salvino; Silva, Emilly Guedes Oliveira e; Passos, Thais Souza; Monteiro, Norberto de Kassio Vieira; https://orcid.org/0000-0002-6460-911XThe study aimed to prospect in silico native and analogous peptides with anti-SARS CoV-2 potential derived from the trypsin inhibitor purified from tamarind seeds (TTIp). From the most stable theoretical model of TTIp (TTIp 56/287), in silico cleavage was performed for the theoretical identification of native peptides and generation of analogous peptides. The anti SARS-CoV-2 potential was investigated through molecular dynamics (MD) simulation between the peptides and binding sites of transmembrane serine protease 2 (TMPRSS2), responsible for the entry of SARS-CoV-2 into the host cell. Five native and analogous peptides were obtained and validated through chemical and physical parameters. The best interaction potential energy (IPE) occurred between TMPRSS2 and one of the native peptides obtained by cleavage with trypsin and its analogous peptide. Thus, both peptides showed many hydrophobic residues, a common physical–chemical property among the peptides that inhibit the entry of enveloped viruses, such as SARS-CoV-2, present in specific drugs to treat COVID-19