Why are Functional Amyloids Non-Toxic in Humans?
AbstractAmyloids 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
Share & Cite This Article
Jackson, M.P.; Hewitt, E.W. Why are Functional Amyloids Non-Toxic in Humans? Biomolecules 2017, 7, 71.
Jackson MP, Hewitt EW. Why are Functional Amyloids Non-Toxic in Humans? Biomolecules. 2017; 7(4):71.Chicago/Turabian Style
Jackson, Matthew P.; Hewitt, Eric W. 2017. "Why are Functional Amyloids Non-Toxic in Humans?" Biomolecules 7, no. 4: 71.
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.