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首页> 外文期刊>Journal of mass spectrometry: JMS >Studies on the cross-interaction between hIAPP and A beta(25-35) and the aggregation process in binary mixture by electrospray ionization-ion mobility-mass spectrometry
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Studies on the cross-interaction between hIAPP and A beta(25-35) and the aggregation process in binary mixture by electrospray ionization-ion mobility-mass spectrometry

机译：用电喷雾电离离子迁移率 - 质谱法研究HIAPP与β（25-35）与β（25-35）的交叉相互作用及二元混合物的聚集过程

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摘要

A wealth of epidemiological evidence indicates a strong link between type 2 diabetes (T2D) and Alzheimer's disease (AD). The fiber deposition with cross-beta-sheet structure formed by self-aggregation and misfolding of amyloidogenic peptides is a common hallmark of both diseases. For the patients with T2D, the fibrils are mainly found in the islets of Langerhans that results from the accumulation of human islet amyloid polypeptide (hIAPP). The major component of aggregates located in the brain of AD patients is amyloid-beta (A beta). Many biophysical and physiological properties are shared by hIAPP and A beta, and both peptides show similar cytotoxic mechanisms. Therefore, it is meaningful to investigate the possible cross-interactions of hIAPP and A beta in both diseases. In this article, the segment 25-35 of A beta was selected because A beta(25-35)was a core region in the process of amyloid formation and showed similar aggregation tendency and toxicity with full-length A beta. The electrospray ionization-ion mobility-mass spectrometry analysis and thioflavin T fluorescence kinetic analysis combined with transmission electron microscopy were used to explore the effects of the coexistence of A beta(25-35)and hIAPP on the self-aggregation of both peptides and whether there was co-assembly in fibrilla tion. The results indicated that the aggregation of hIAPP and A beta(25-35) had two nucleation stages in the binary mixtures. hIAPP and A beta(25-35) had a high binding affinity and a series of hetero-oligomers formed in the mixtures of hIAPP and A beta(25-35) in the early stage. The cross-reaction between hIAPP monomers and A beta(25-35) monomers as well as a little of oligomers during primary nucleation stage could accelerate the aggregation of A beta(25-35). However, owing to the obvious difference in aggregation ability between hIAPP and A beta(25-35), this cross-interaction had no significant impact on the self-assembly of hIAPP. Our study may offer a better understanding for exploring the molecular mechanism of the association between AD and T2D observed in clinical and epidemiological studies and developing therapeutic strategies against amyloid diseases.
机译：丰富的流行病学证据表明2型糖尿病（T2D）和阿尔茨海默病（AD）之间存在强烈的联系。通过自聚集形成和淀粉样蛋白肽的误用和错误折叠形成的纤维沉积是两种疾病的共同标志。对于T2D的患者，原纤维主要发现在朗格汉斯的胰岛中，这是由人胰岛淀粉样蛋白多肽（HIAPP）的积累产生的。位于AD患者脑中的聚集体的主要成分是淀粉样蛋白β（β）。通过HIAPP和β共享许多生物物理和生理性质，并且两种肽都显示出类似的细胞毒性机制。因此，研究HIAPP和β在两种疾病中的可能交叉相互作用是有意义的。在本文中，选择了β的段25-35，因为β（25-35）是淀粉样蛋白形成过程中的核心区域，并且显示出类似的聚集趋势和具有全长β的毒性。电喷雾电离离子迁移率 - 质谱分析和硫蛋白T荧光动力学分析与透射电子显微镜结合使用，探讨了β（25-35）和HIAPP对肽的自我聚集的影响，以及是否在纤维状中有共同组装。结果表明，HIAPP和β（25-35）的聚集在二元混合物中具有两个成核阶段。 HIAPP和β（25-35）具有高结合亲和力，并且在早期的阶段中形成了在HIAPP和β（25-35）的混合物中形成的杂寡值聚合物。在初级成核期期间HiaPP单体和β（25-35）单体以及少量低聚物之间的交叉反应可以加速β（25-35）的聚集。然而，由于HIAPP和β（25-35）之间的聚集能力的显而易见，这种交叉互动对HIAPP的自组装没有显着影响。我们的研究可以更好地理解探索临床和流行病学研究中观察到的AD和T2D关联的分子机制，以及对淀粉样疾病的治疗策略发展治疗策略。

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  • 来源
    《Journal of mass spectrometry: JMS》 |2020年第10期|共10页
  • 作者

    Pang Bo; Zhuang Xiaoyu; Bian Xinyu; Liu Shu; Liu Zhiqiang; Song Fengrui;

  • 作者单位

    Chinese Acad Sci Changchun Inst Appl Chem Natl Ctr Mass Spectrometry Changchun State Key La Jilin Prov Key Lab Chinese Med Chem &

    Mass Spectr Changchun Peoples R China;

    Shanghai Univ Tradit Chinese Med Expt Ctr Sci &

    Technol Shanghai 201203 Peoples R China;

    Chinese Acad Sci Changchun Inst Appl Chem Natl Ctr Mass Spectrometry Changchun State Key La Jilin Prov Key Lab Chinese Med Chem &

    Mass Spectr Changchun Peoples R China;

    Chinese Acad Sci Changchun Inst Appl Chem Natl Ctr Mass Spectrometry Changchun State Key La Jilin Prov Key Lab Chinese Med Chem &

    Mass Spectr Changchun Peoples R China;

    Chinese Acad Sci Changchun Inst Appl Chem Natl Ctr Mass Spectrometry Changchun State Key La Jilin Prov Key Lab Chinese Med Chem &

    Mass Spectr Changchun Peoples R China;

    Chinese Acad Sci Changchun Inst Appl Chem Natl Ctr Mass Spectrometry Changchun State Key La Jilin Prov Key Lab Chinese Med Chem &

    Mass Spectr Changchun Peoples R China;

  • 收录信息
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类 分析化学;
  • 关键词

    aggregation; Alzheimer's disease; amyloid-beta(25-35); human islet amyloid polypeptide; interaction; ion mobility-mass spectrometry; type 2 diabetes;

    机译：聚集;阿尔茨海默病;淀粉样蛋白β（25-35）;人胰岛淀粉样蛋白多肽;相互作用;离子迁移率 - 质谱;2型糖尿病;

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