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首页> 外文期刊>RSC Advances >Characterization of insulin cross-seeding: the underlying mechanism reveals seeding and denaturant-induced insulin fibrillation proceeds through structurally similar intermediates
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Characterization of insulin cross-seeding: the underlying mechanism reveals seeding and denaturant-induced insulin fibrillation proceeds through structurally similar intermediates

机译：胰岛素交叉播种的表征：潜在机制揭示播种和变性剂诱导的胰岛素颤动通过结构相似的中间体进行

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摘要

Insulin rapidly fibrillates in the presence of amyloid seeds from different sources. To address its cross-reactivity we chose the seeds of seven model proteins and peptides along with the seeds of insulin itself. Model candidates were selected/designed according to their size, amino acid sequence, and hydrophobicity. We found while some seeds provided catalytic ends for inducing the formation of non-native insulin conformers and increase fibrillation, others attenuated insulin fibrillation kinetics. We also observed competition between the intermediate insulin conformers which formed with urea and amyloid seeds in entering the fibrillogenic pathway. Simultaneous incubation of insulin with urea and amyloid seeds resulted in the formation of nearly similar insulin intermediate conformers which synergistically enhance insulin fibrillation kinetics. Given these results, it is highly likely that, structurally, there is a specific intermediate in different pathways of insulin fibrillation that governs fibrillation kinetics and morphology of the final mature fibril. Overall, this study provides a novel mechanistic insight into insulin fibrillation and gives new information on how seeds of different proteins are capable of altering insulin fibrillation kinetics and morphology. This report, for the first time, tries to answer an important question that why fibrillation of insulin is either accelerated or attenuated in the presence of amyloid fibril seeds from different sources.
机译：胰岛素在来自不同来源的淀粉样蛋白种子存在下迅速纤维素。为了解决其交叉反应性，我们选择七种模型蛋白和肽的种子以及胰岛素本身的种子。根据其尺寸，氨基酸序列和疏水性选择模型候选者。我们发现，虽然一些种子提供了用于诱导非天然胰岛素簇的形成并增加纤维化的催化末端，但是其他种子抑制胰岛素的胰岛素颤动动力学。我们还观察到在进入纤维原途径时形成的中间胰岛素赋板与尿素和淀粉样液形成的竞争。同时孵育尿素和淀粉样种子的胰岛素导致近似相似的胰岛素中间塑壳，其协同增强胰岛素原纤化动力学。鉴于这些结果，很可能在结构上，在结构上，在胰岛素颤动的不同途径中存在特异的中间体，其治理了最终成熟原纤维的原纤化动力学和形态。总体而言，本研究提供了一种新颖的机械洞察胰岛素颤动，并提供有关不同蛋白质的种子能够改变胰岛素颤动动力学和形态学的新信息。本报告首次试图回答重要的问题：为什么胰岛素的原纤化在来自不同来源的淀粉样蛋白原纤维种子存在下加速或减弱。

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  • 来源
    《RSC Advances》 |2020年第50期|共15页
  • 作者

    Akbarian Mohsen; Kianpour Maryam; Yousefi Reza; Moosavi-Movahedi Ali Akbar;

  • 作者单位

    Shiraz Univ Coll Sci Dept Biol Prot Chem Lab PCL Shiraz Iran;

    Shiraz Univ Coll Sci Dept Biol Prot Chem Lab PCL Shiraz Iran;

    Shiraz Univ Coll Sci Dept Biol Prot Chem Lab PCL Shiraz Iran;

    Univ Tehran Inst Biochem &

    Biophys IBB Tehran Iran;

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  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类 化学;
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