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Fibrils from designed non-amyloid-related synthetic peptides induce AA-amyloidosis during inflammation in an animal model
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Genetics and Pathology.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Cell Biology.
2009 (English)In: PloS one, ISSN 1932-6203, Vol. 4, no 6, e6041- p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2009. Vol. 4, no 6, e6041- p.
National Category
Medical and Health Sciences
URN: urn:nbn:se:uu:diva-124449DOI: 10.1371/journal.pone.0006041ISI: 000267515700002PubMedID: 19582162OAI: oai:DiVA.org:uu-124449DiVA: diva2:317554
Available from: 2010-05-04 Created: 2010-05-04 Last updated: 2010-12-20Bibliographically approved

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Westermark, Per
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