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Journal Articles ACS Chemical Neuroscience Year : 2023

Discrimination between Alpha-Synuclein Protein Variants with a Single Nanometer-Scale Pore

Abstract

Alpha-synuclein is one of several key factors in the regulation of nerve activity. It is striking that single- or multiple-point mutations in the 140-amino-acid-long protein can change its structure, which leads to the protein’s aggregation and fibril formation (which is associated with several neurodegenerative diseases, e.g., Parkinson’s disease). We recently demonstrated that a single nanometer-scale pore can identify proteins based on its ability to discriminate between protease-generated polypeptide fragments. We show here that a variation of this method can readily discriminate between the wild-type alpha synuclein, a known deleterious point mutation of the glutamic acid at position 46 replaced with a lysine (E46K), and post-translational modifications (i.e., tyrosine Y39 nitration and serine 129 phosphorylation).
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Dates and versions

hal-04154813 , version 1 (28-11-2023)

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Mazdak Afshar Bakshloo, Safia Yahiaoui, Matthieu Bourderioux, Régis Daniel, Manuela Pastoriza-Gallego, et al.. Discrimination between Alpha-Synuclein Protein Variants with a Single Nanometer-Scale Pore. ACS Chemical Neuroscience, 2023, 14 (14), pp.2517-2526. ⟨10.1021/acschemneuro.3c00164⟩. ⟨hal-04154813⟩
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