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Apoferritin Protein Amyloid Fibrils with Tunable Chirality and Polymorphism

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    Apoferritin Protein Amyloid Fibrils with Tunable Chirality and Polymorphism
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    Journal of the American Chemical Society

    Cite this: J. Am. Chem. Soc. 2019, 141, 4, 1606–1613
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    https://doi.org/10.1021/jacs.8b11418
    Published December 27, 2018
    Copyright © 2018 American Chemical Society
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    Abstract

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    Ferritin, a soluble and highly robust protein with subunits packed into well-defined helices, is a key component of the iron regulatory system in the brain and thus is widely recognized as a crucial protein for iron metabolism, but may also bear possible implications in some neurodegenerative disorders. Here, we present evidence of how human recombinant apoferritin can convert into an unusual structure from its folded native state; that is, amyloid fibrils analogue to those found in pathological disorders such as Alzheimer’s and Parkinson’s diseases. An extensive combination of advanced microscopy, spectroscopy and scattering techniques concur to reveal that apoferritin fibrils possess a common double stranded twisted ribbon structure which can result in a mesoscopic right-handed chirality. We highlight a direct connection between the chirality and morphology of the resulting amyloid fibrils, and the initial protein subunits composition, advancing our understanding on the possible role of misfolding in some ferritin-related pathologies and posing new bases for the design of chiral 1D functional nanostructures.

    Copyright © 2018 American Chemical Society

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    Supporting Information

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    The Supporting Information is available free of charge on the ACS Publications website at DOI: 10.1021/jacs.8b11418.

    • Full experimental methods; additional characterizations presented: TEM images, AFM images and structural characterization of APO fibrils; CD spectra, FTIR spectra, WAXS scattering profile, SDS-PAGE electrophoresis and MS spectra for APO fibrils; FLIM-PIE imaging of APO aggregates; TEM images, AFM images and SDS-PAGE electrophoresis of functionalized L-rich APO fibrils; additional FLIM-PIE results on functionalized human L-APO and H-APO aggregates (PDF)

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    Cited By

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    This article is cited by 23 publications.

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    Journal of the American Chemical Society

    Cite this: J. Am. Chem. Soc. 2019, 141, 4, 1606–1613
    Click to copy citationCitation copied!
    https://doi.org/10.1021/jacs.8b11418
    Published December 27, 2018
    Copyright © 2018 American Chemical Society
    Request reuse permissions

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