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Aggregation and fibril morphology of the Arctic mutation of Alzheimer's Aβ peptide by CD, TEM, STEM and in situ AFM
Luleå University of Technology, Department of Engineering Sciences and Mathematics, Material Science.
Luleå University of Technology.
Luleå University of Technology, Department of Civil, Environmental and Natural Resources Engineering, Sustainable Process Engineering. Department of Physics, Kazan State University, Kazan, Russia.ORCID iD: 0000-0002-6810-1882
Laboratory of Bioengineering and Physical Science, National Institute of Biomedical Imaging and Bioengineering, National Institutes of Health, Bethesda, USA.
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2012 (English)In: Journal of Structural Biology, ISSN 1047-8477, E-ISSN 1095-8657, Vol. 180, no 1, p. 174-189Article in journal (Refereed) Published
Abstract [en]

Morphology of aggregation intermediates, polymorphism of amyloid fibrils and aggregation kinetics of the "Arctic" mutant of the Alzheimer's amyloid β-peptide, Aβ (1-40)(E22G), in a physiologically relevant Tris buffer (pH 7.4) were thoroughly explored in comparison with the human wild type Alzheimer's amyloid peptide, wt-Aβ (1-40), using both in situ atomic force and electron microscopy, circular dichroism and thioflavin T fluorescence assays. For arc-Aβ (1-40) at the end of the 'lag'-period of fibrillization an abrupt appearance of ∼3 nm size 'spherical aggregates' with a homogeneous morphology, was identified. Then, the aggregation proceeds with a rapid growth of amyloid fibrils with a variety of morphologies, while the spherical aggregates eventually disappeared during in situ measurements. Arc-Aβ (1-40) was also shown to form fibrils at much lower concentrations than wt-Aβ (1-40): ≤2.5 μM and 12.5 μM, respectively. Moreover, at the same concentration, 50 μM, the aggregation process proceeds more rapidly for arc-Aβ (1-40): the first amyloid fibrils were observed after c.a. 72 h from the onset of incubation as compared to approximately 7 days for wt-Aβ (1-40). Amyloid fibrils of arc-Aβ (1-40) exhibit a large variety of polymorphs, at least five, both coiled and non-coiled distinct fibril structures were recognized by AFM, while at least four types of arc-Aβ (1-40) fibrils were identified by TEM and STEM and their mass-per-length statistics were collected suggesting supramolecular structures with two, four and six β-sheet laminae. Our results suggest a pathway of fibrillogenesis for full-length Alzheimer's peptides with small and structurally ordered transient spherical aggregates as on-pathway immediate precursors of amyloid fibrils.

Place, publisher, year, edition, pages
2012. Vol. 180, no 1, p. 174-189
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Other Physics Topics Physical Chemistry
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Experimental Physics; Chemistry of Interfaces
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URN: urn:nbn:se:ltu:diva-12848DOI: 10.1016/j.jsb.2012.06.010ISI: 000310046400020PubMedID: 22750418Scopus ID: 2-s2.0-84866988080Local ID: bfea934d-f775-415b-8e89-4ba68ada9687OAI: oai:DiVA.org:ltu-12848DiVA, id: diva2:985799
Note

Validerad; 2012; 20120806 (ysko)

Available from: 2016-09-29 Created: 2016-09-29 Last updated: 2023-09-05Bibliographically approved

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Norlin, NilsFilippov, AndreiAlmqvist, NilsAntzutkin, Oleg

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