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The modification of amyloid fibrils cytotoxicity through exogenous nanomaterials is crucial to understand the processes controlling the role of protein aggregation in the related diseases. The influence of nanoparticles on amyloid stability yields great interest due to the small size and high surface area-to-volume ratio of nanoparticles. Various physico-chemical parameters play a role in the interaction of proteins and nanoparticles in solution, thus influencing the disaggregation of preformed fibrils. We have examined the influence of two kinds of metallic nanoparticles on lysozyme amyloid fibrils using a multi-technique approach and focalized their impact on cytotoxicity on human neuroblastoma cells (SH-SY5Y). In particular, fluorescence, infrared and circular dichroism spectroscopies, optical and atomic force microscopy experiments have been carried out; the results are analyzed to rationalize the effects of these complexes on neural cell viability. It is remarkable, that the fibrils in the presence of AuNPs, unlike fibrils alone or with AgNPs, do not generate a significant cytotoxic effect even at high concentration and an amyloid degradation effect is visible.

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Publication history
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Acknowledgements

Publication history

Received: 28 November 2019
Revised: 14 February 2020
Accepted: 10 March 2020
Published: 14 April 2020
Issue date: April 2020

Copyright

© Tsinghua University Press and Springer-Verlag GmbH Germany, part of Springer Nature 2020

Acknowledgements

This work was partially supported by Slovak grand agency VEGA 2/0145/17, APVV-18-0284, Italian flagship NANOMAX, N-CHEM, Ministery of Education, University and Research (PRIN grant 20173L7W8K). Microscopy was carried out at the SPM@ISMN facility.

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