由螺旋中间体制备的α-突触核蛋白多晶体的固态核磁共振分配。

IF 0.8 4区 生物学 Q4 BIOPHYSICS Biomolecular NMR Assignments Pub Date : 2024-07-04 DOI:10.1007/s12104-024-10188-0
Sahil Ahlawat, Surabhi Mehra, Chandrakala M. Gowda, Samir K Maji, Vipin Agarwal
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引用次数: 0

摘要

突触核蛋白病是一种神经退行性疾病,其特征是α-突触核蛋白蛋白聚集在神经元和神经胶质细胞中。体内和体外α-突触核蛋白纤维都倾向于表现出多态性。多态性导致源自单个多肽/蛋白质的纤维结构发生变化。多态性通常具有不同的生物物理、生物化学和致病特性。一种疾病的各种病理现象可能与不同的多态性有关。同样,在不同的突触核蛋白病中,每种病症都可能与不同的多态性有关。纤维的形成是一个成核依赖过程,涉及从单体形成瞬时和异质的中间体。由于不同条件下的选择机制不同,多态性被认为是由异质的低聚物群体产生的。为了验证这一假设,我们分离并培养了α-突触核蛋白体外纤维化过程中的不同中间产物,以形成不同的多态性。在此,我们利用固态核磁共振谱报告了由螺旋中间体制备的纤维的 13C 和 15N 化学位移和二级结构。
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Solid-state NMR assignment of α-synuclein polymorph prepared from helical intermediate

Synucleinopathies are neurodegenerative diseases characterized by the accumulation of α-synuclein protein aggregates in the neurons and glial cells. Both ex vivo and in vitro α-synuclein fibrils tend to show polymorphism. Polymorphism results in structure variations among fibrils originating from a single polypeptide/protein. The polymorphs usually have different biophysical, biochemical and pathogenic properties. The various pathologies of a single disease might be associated with distinct polymorphs. Similarly, in the case of different synucleinopathies, each condition might be associated with a different polymorph. Fibril formation is a nucleation-dependent process involving the formation of transient and heterogeneous intermediates from monomers. Polymorphs are believed to arise from heterogeneous oligomer populations because of distinct selection mechanisms in different conditions. To test this hypothesis, we isolated and incubated different intermediates during in vitro fibrillization of α-synuclein to form different polymorphs. Here, we report 13C and 15N chemical shifts and the secondary structure of fibrils prepared from the helical intermediate using solid-state nuclear magnetic spectroscopy.

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来源期刊
Biomolecular NMR Assignments
Biomolecular NMR Assignments 生物-光谱学
CiteScore
1.70
自引率
11.10%
发文量
59
审稿时长
6-12 weeks
期刊介绍: Biomolecular NMR Assignments provides a forum for publishing sequence-specific resonance assignments for proteins and nucleic acids as Assignment Notes. Chemical shifts for NMR-active nuclei in macromolecules contain detailed information on molecular conformation and properties. Publication of resonance assignments in Biomolecular NMR Assignments ensures that these data are deposited into a public database at BioMagResBank (BMRB; http://www.bmrb.wisc.edu/), where they are available to other researchers. Coverage includes proteins and nucleic acids; Assignment Notes are processed for rapid online publication and are published in biannual online editions in June and December.
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