Half a century of amyloids: past, present and future

Ke, Pu Chun, Zhou, Ruhong, Serpell, Louise C, Riek, Roland, Knowles, Tuomas P J, Lashuel, Hilal A, Gazit, Ehud, Hamley, Ian W, Davis, Thomas P, Fändrich, Marcus, Otzen, Daniel Erik, Chapman, Matthew R, Dobson, Christopher M, Eisenberg, David S and Mezzenga, Raffaele (2020) Half a century of amyloids: past, present and future. Chemical Society Reviews, 49 (15). pp. 5473-5509. ISSN 0306-0012

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Amyloid diseases are global epidemics with profound health, social and economic implications and yet remain without a cure. This dire situation calls for research into the origin and pathological manifestations of amyloidosis to stimulate continued development of new therapeutics. In basic science and engineering, the cross-ß architecture has been a constant thread underlying the structural characteristics of pathological and functional amyloids, and realizing that amyloid structures can be both pathological and functional in nature has fuelled innovations in artificial amyloids, whose use today ranges from water purification to 3D printing. At the conclusion of a half century since Eanes and Glenner's seminal study of amyloids in humans, this review commemorates the occasion by documenting the major milestones in amyloid research to date, from the perspectives of structural biology, biophysics, medicine, microbiology, engineering and nanotechnology. We also discuss new challenges and opportunities to drive this interdisciplinary field moving forward. This journal is

Item Type: Article
Keywords: Alzheimer Disease, Amyloid, Amyloidosis, Cations, Divalent, Cross-Linking Reagents, Humans, Models, Molecular, Molecular Conformation, Printing, Three-Dimensional, Protein Folding, Protein Processing, Post-Translational
Schools and Departments: School of Life Sciences > Neuroscience
SWORD Depositor: Mx Elements Account
Depositing User: Mx Elements Account
Date Deposited: 17 Sep 2021 13:44
Last Modified: 04 Oct 2021 09:51
URI: http://sro.sussex.ac.uk/id/eprint/101724

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