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Biomolecules 2017, 7(4), 71; doi:10.3390/biom7040071

Why are Functional Amyloids Non-Toxic in Humans?

School of Molecular and Cellular Biology and Astbury Centre for Structural Molecular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UK
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Academic Editors: Margaret Sunde, Matthew Chapman, Daniel Otzen and Sarah Perrett
Received: 21 July 2017 / Revised: 18 September 2017 / Accepted: 20 September 2017 / Published: 22 September 2017
(This article belongs to the Special Issue Functional Amyloids)
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Abstract

Amyloids were first identified in association with amyloidoses, human diseases in which proteins and peptides misfold into amyloid fibrils. Subsequent studies have identified an array of functional amyloid fibrils that perform physiological roles in humans. Given the potential for the production of toxic species in amyloid assembly reactions, it is remarkable that cells can produce these functional amyloids without suffering any obvious ill effect. Although the precise mechanisms are unclear, there are a number of ways in which amyloid toxicity may be prevented. These include regulating the level of the amyloidogenic peptides and proteins, minimising the production of prefibrillar oligomers in amyloid assembly reactions, sequestrating amyloids within membrane bound organelles, controlling amyloid assembly by other molecules, and disassembling the fibrils under physiological conditions. Crucially, a better understanding of how toxicity is avoided in the production of functional amyloids may provide insights into the prevention of amyloid toxicity in amyloidoses. View Full-Text
Keywords: amyloids; fibril; oligomers; toxicity; functional amyloid amyloids; fibril; oligomers; toxicity; functional amyloid
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Jackson, M.P.; Hewitt, E.W. Why are Functional Amyloids Non-Toxic in Humans? Biomolecules 2017, 7, 71.

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