Real-time monitoring of amyloid fibrillation by electrical impedance spectroscopy

Silva, Rafael R. da; Lima, Sandro V. de; Melo, Celso P. de; Frías, Isaac A.M.; Oliveira, Maria D.L.; Andrade, César A.S.

doi:10.1016/j.colsurfb.2017.10.010

Cited by 3 publications

(3 citation statements)

References 47 publications

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“…In addition, XPD on lysozyme particulates showed amyloid-like features, with a powder ring at 4.7 Å and a faint, broad signal at around 9.5 Å (Figure S3), in agreement with a previous report . These ThT fluorescence, FTIR, and XPD results confirm that lysozyme particulates are enriched in β-sheets, yet it remains unclear whether the latter are of purely amyloid nature or not …”

supporting

confidence: 91%

“…11 Similarly, small-angle neutron scattering (SANS 12 ) can be used to study protein amyloidogenesis 13 and aggregation. 14 Electric impedance spectroscopy 15 and dielectric relaxation spectroscopy 16 are also sensitive to amyloid aggregation. Nuclear magnetic resonance (NMR), in contrast, provides exquisite structural and dynamic information on amyloid fibrils 17,18 but cannot follow the entire aggregation process in real time.…”

mentioning

confidence: 99%

“…29 These ThT fluorescence, FTIR, and XPD results confirm that lysozyme particulates are enriched in β-sheets, yet it remains unclear whether the latter are of purely amyloid nature or not. 15 Neutron spectroscopy experiments were carried out at the IN16B backscattering spectrometer 30,31 of the Institut Laue Langevin (ILL) in Grenoble, France. To characterize the initial state, we measured quasi-elastic neutron scattering (QENS) spectra at 7 °C (see Methods in the Supporting Information).…”

mentioning

confidence: 99%

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

Pounot

Chaaban

Foderà

et al. 2020

J. Phys. Chem. Lett.

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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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confidence: 91%