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Tracking Internal and Global Diffusive Dynamics During Protein Aggregation by High-Resolution Neutron Spectroscopy

Abstract : Proteins can misfold and form either amorphous or organized aggregates with different morphologies and features. Aggregates of amyloid nature are pathological hallmarks in so-called protein conformational diseases, including Alzheimer's and Parkinson's. Evidence prevails that the transient early phases of the reaction determine the aggregate morphology and toxicity. As a consequence, real-time monitoring of protein aggregation is of utmost importance. Here, we employed time-resolved neutron backscattering spectroscopy to follow center-of-mass self-diffusion and nano- to picosecond internal dynamics of lysozyme during aggregation into a specific β-sheet rich superstructure, called particulates, formed at the isoelectric point of the protein. Particulate formation is found to be a one-step process, and protein internal dynamics, to remain unchanged during the entire aggregation process. The time-resolved neutron backscattering spectroscopy approach developed here, in combination with standard kinetics assays, provides a unifying framework in which dynamics and conformational transitions can be related to the different aggregation pathways.
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https://hal.univ-grenoble-alpes.fr/hal-02947747
Contributeur : Frank Thomas <>
Soumis le : jeudi 24 septembre 2020 - 09:54:11
Dernière modification le : mercredi 14 octobre 2020 - 04:04:43

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Kevin Pounot, Hussein Chaaban, Vito Foderà, Giorgio Schirò, Martin Weik, et al.. Tracking Internal and Global Diffusive Dynamics During Protein Aggregation by High-Resolution Neutron Spectroscopy. Journal of Physical Chemistry Letters, American Chemical Society, 2020, 11 (15), pp.6299-6304. ⟨10.1021/acs.jpclett.0c01530⟩. ⟨hal-02947747⟩

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