The aim of this study was to prospect 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 hydrolysis to assess its susceptibility to enzymatic degradation and determine suitable enzymes for cleavage . The theoretical model was established to assess the purified tamarind seed trypsin inhibitor (TTIp 56/287) being cleaved 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 mol-1). 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 .

中文翻译：

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胰岛素受体与从罗望子种子中纯化的胰蛋白酶抑制剂衍生的肽之间的相互作用：胰岛素样肽的计算机筛选

本研究的目的是探索源自多功能蛋白的肽并评估它们与胰岛素受体 (IR) 的相互作用。通过胰蛋白酶-琼脂糖4B-CNBr亲和层析获得从罗望子种子（TTI）中分离的胰蛋白酶抑制剂，并随后进行表征。 TTI 经过水解以评估其对酶促降解的敏感性并确定合适的酶进行切割。建立理论模型来评估纯化的罗望子种子胰蛋白酶抑制剂（TTIp 56/287）被切割并选择用于分子动力学模拟。在生成的肽中，Peptidetripquimo59 与 IR 的对接分数最高 (-175.53)，表明在复合物形成中具有很强的亲和力和稳定性。观察到关键残基与 IR 存在显着相互作用，包括精氨酸 16 (-209.07 kJ mol-1)、苏氨酸 1 (-148.54 kJ mol-1) 和缬氨酸 2 (-94.53 kJ mol-1)。此外，还发现胰岛素和 Peptidetripquimo59 均表现出与胰岛素受体 (IR) 上相同位置的结合。半经验方法的结果表明，与胰岛素-IR 复合物等其他复合物相比，Peptidetripquimo59 表现出更大的与 IR 相互作用的潜力，表明它可以作为开发针对 1 型和 2 型的治疗药物的起点。 2 糖尿病。