Next Article in Journal
Peptidylprolyl Isomerases as In Vivo Carriers for Drugs That Target Various Intracellular Entities
Next Article in Special Issue
The Production of Curli Amyloid Fibers Is Deeply Integrated into the Biology of Escherichia coli
Previous Article in Journal / Special Issue
The Physiological and Pathological Implications of the Formation of Hydrogels, with a Specific Focus on Amyloid Polypeptides
Article Menu

Export Article

Open AccessReview
Biomolecules 2017, 7(4), 71;

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
Author to whom correspondence should be addressed.
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)
Full-Text   |   PDF [1053 KB, uploaded 25 September 2017]   |  


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

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

Share & Cite This Article

MDPI and ACS Style

Jackson, M.P.; Hewitt, E.W. Why are Functional Amyloids Non-Toxic in Humans? Biomolecules 2017, 7, 71.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Biomolecules EISSN 2218-273X Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top