Apoferritin Protein Amyloid Fibrils with Tunable Chirality and Polymorphism Jurado Palomares, Rocío González-Vera, Juan A. Ruiz Arias, Álvaro Domínguez Vera, José Manuel Orte Gutiérrez, Ángel Gálvez, Natividad 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. 2024-11-19T07:28:12Z 2024-11-19T07:28:12Z 2019 journal article https://hdl.handle.net/10481/97037 10.1021/jacs.8b11418 eng open access American Chemical Society