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首页> 外文期刊>Journal of Molecular Biology >Ion mobility separation coupled with MS detects two structural states of Alzheimer's disease Abeta1-40 peptide oligomers.
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Ion mobility separation coupled with MS detects two structural states of Alzheimer's disease Abeta1-40 peptide oligomers.

机译：离子淌度分离与MS结合检测阿尔茨海默氏病Abeta1-40肽寡聚物的两个结构状态。

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Mounting evidence points to the soluble oligomers of amyloid beta (Abeta) peptide as important neurotoxic species in Alzheimer's disease, causing synaptic dysfunction and neuronal injury, and finally leading to neuronal death. The mechanism of the Abeta peptide self-assembly is still under debate. Here, Abeta1-40 peptide oligomers were studied using mass spectrometry combined with ion mobility spectrometry, which allowed separation of the signals of numerous oligomers and measurement of their collisional cross-section values (Omega). For several oligomers, at least two different species of different Omega values were detected, indicating the presence of at least two families of conformers: compact and extended. The obtained results are rationalized by a set of molecular models of Abeta1-40 oligomer structure that provided a very good correlation between the experimental and theoretical Omega values, both for the compact and the extended forms. Our results indicate that mass spectrometry detects oligomeric species that are on-pathway in the process of fibril formation or decay, but also alternative structures which may represent off-pathway evolution of oligomers.
机译：越来越多的证据表明，淀粉样β（Abeta）肽的可溶性寡聚体是阿尔茨海默氏病中重要的神经毒性物种，可引起突触功能障碍和神经元损伤，并最终导致神经元死亡。 Abeta肽自组装的机制仍在争论中。在这里，使用质谱与离子迁移谱结合的方法研究了Abeta1-40肽寡聚物，该技术可以分离众多寡聚物的信号并测量其碰撞截面值（Omega）。对于几种寡聚物，检测到至少两种不同的Omega值不同的物种，表明存在至少两个构象异构体家族：紧密和扩展。所获得的结果通过Abeta1-40低聚物结构的分子模型集进行了合理化，该模型在紧凑和扩展形式的实验和理论Omega值之间都提供了很好的相关性。我们的结果表明，质谱检测到的是在原纤维形成或衰变过程中正在传播的寡聚物种，而且还可以检测到可能代表寡聚体非进化进化的替代结构。

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