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Amyloid particles facilitate surface-catalyzed cross-seeding by acting as promiscuous nanoparticles

Koloteva-Levine, Nadejda, Aubrey, Liam D., Marchante, Ricardo, Purton, Tracey J, Hiscock, Jennifer R., Tuite, Mick F., Xue, Wei-Feng (2021) Amyloid particles facilitate surface-catalyzed cross-seeding by acting as promiscuous nanoparticles. Proceedings of the National Academy of Sciences of the United States of America, 118 (36). Article Number 2104148118. ISSN 0027-8424. (doi:10.1073/pnas.2104148118) (KAR id:90111)

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Amyloid seeds are nanometer-sized protein particles that accelerate amyloid assembly as well as propagate and transmit the amyloid protein conformation associated with a wide range of protein misfolding diseases. However, seeded amyloid growth through templated elongation at fibril ends cannot explain the full range of molecular behaviors observed during cross-seeded formation of amyloid by heterologous seeds. Here, we demonstrate that amyloid seeds can accelerate amyloid formation via a surface catalysis mechanism without propagating the specific amyloid conformation associated with the seeds. This type of seeding mechanism is demonstrated through quantitative characterization of the cross-seeded assembly reactions involving two nonhomologous and unrelated proteins: the human Aβ42 peptide and the yeast prion–forming protein Sup35NM. Our results demonstrate experimental approaches to differentiate seeding by templated elongation from nontemplated amyloid seeding and rationalize the molecular mechanism of the cross-seeding phenomenon as a manifestation of the aberrant surface activities presented by amyloid seeds as nanoparticles.

Item Type: Article
DOI/Identification number: 10.1073/pnas.2104148118
Uncontrolled keywords: protein aggregation and assembly, Sup35 yeast prion protein, amyloid β peptide, atomic force microscopy, Saccharomyces cerevisiae
Subjects: Q Science
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: Wei-Feng Xue
Date Deposited: 09 Sep 2021 14:47 UTC
Last Modified: 15 Mar 2022 23:10 UTC
Resource URI: (The current URI for this page, for reference purposes)
Marchante, Ricardo:
Hiscock, Jennifer R.:
Tuite, Mick F.:
Xue, Wei-Feng:
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