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

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Afshar Bakshloo, Mazdak | Yahiaoui, Safia | Bourderioux, Matthieu | Daniel, Régis | Pastoriza-Gallego, Manuela | Kasianowicz, John | Oukhaled, Abdelghani

Edité par CCSD ; American Chemical Society (ACS) -

International audience. 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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