Fibrils from designed non-amyloid-related synthetic peptides induce AA-amyloidosis during inflammation in an animal model
2009 (English)In: PLoS ONE, ISSN 1932-6203, Vol. 4, no 6, e6041- p.Article in journal (Refereed) Published
Background: Mouse AA-amyloidosis is a transmissible disease by a prion-like mechanism where amyloid fibrils act by seeding. Synthetic peptides with no amyloid relationship can assemble into amyloid-like fibrils and these may have seeding capacity for amyloid proteins. Principal Findings: Several synthetic peptides, designed for nanotechnology, have been examined for their ability to produce fibrils with Congo red affinity and concomitant green birefringence, affinity for thioflavin S and to accelerate AA-amyloidosis in mice. It is shown that some amphiphilic fibril-forming peptides not only produced Congo red birefringence and showed affinity for thioflavin S, but they also shortened the lag phase for systemic AA-amyloidosis in mice when they were given intravenously at the time of inflammatory induction with silver nitride. Peptides, not forming amyloid-like fibrils, did not have such properties. Conclusions: These observations should caution researchers and those who work with synthetic peptides and their derivatives to be aware of the potential health concerns. © 2009 Westermark et al.
Place, publisher, year, edition, pages
2009. Vol. 4, no 6, e6041- p.
Medical and Health Sciences
IdentifiersURN: urn:nbn:se:liu:diva-21313DOI: 10.1371/journal.pone.0006041OAI: oai:DiVA.org:liu-21313DiVA: diva2:241054
P. Westermark, Katarzyna Lundmark and Gunilla Westermark, Fibrils from designed non-amyloid-related synthetic peptides induce AA-amyloidosis during inflammation in an animal model, 2009, PLoS ONE, (4), 6, e6041.