Searching for just a few words should be enough to get started. If you need to make more complex queries, use the tips below to guide you.
Article type: Research Article
Authors: Selivanova, Olga M.a; 1 | Surin, Alexey K.a; b; 1 | Marchenkov, Victor V.a | Dzhus, Ulyana F.a | Grigorashvili, Elizaveta I.a | Suvorina, Mariya Yu.a | Glyakina, Anna V.a; c | Dovidchenko, Nikita V.a | Galzitskaya, Oxana V.a; *
Affiliations: [a] Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, Russia | [b] State Research Center for Applied Microbiology & Biotechnology, Obolensk, Serpukhov District, Moscow Region, Russia | [c] Institute of Mathematical Problems of Biology, Pushchino, Moscow Region, Russia
Correspondence: [*] Correspondence to: O.V. Galzitskaya, Institute of Protein Research, Russian Academy of Sciences, Pushchino, Russia. Tel.: +7 4967 318275; Fax: +7 4967 318435; E-mail: [email protected].
Note: [1] These authors contributed equally to this work.
Abstract: It has been demonstrated using Aβ40 and Aβ42 recombinant and synthetic peptides that their fibrils are formed of complete oligomer ring structures. Such ring structures have a diameter of about 8-9 nm, an oligomer height of about 2– 4 nm, and an internal diameter of the ring of about 3-4 nm. Oligomers associate in a fibril in such a way that they interact with each other, overlapping slightly. There are differences in the packing of oligomers in fibrils of recombinant and synthetic Aβ peptides. The principal difference is in the degree of orderliness of ring-like oligomers that leads to generation of morphologically different fibrils. Most ordered association of ring-like structured oligomers is observed for a recombinant Aβ40 peptide. Less ordered fibrils are observed with the synthetic Aβ42 peptide. Fragments of fibrils the most protected from the action of proteases have been determined by tandem mass spectrometry. It was shown that unlike Aβ40, fibrils of Aβ42 are more protected, showing less ordered organization compared to that of Aβ40 fibrils. Thus, the mass spectrometry data agree with the electron microscopy data and structural models presented here.
Keywords: Aβ42 and Aβ40 peptides, Alzheimer’s disease, amyloid fibrils, polymorphism, ring-like oligomers
DOI: 10.3233/JAD-160405
Journal: Journal of Alzheimer's Disease, vol. 54, no. 2, pp. 821-830, 2016
IOS Press, Inc.
6751 Tepper Drive
Clifton, VA 20124
USA
Tel: +1 703 830 6300
Fax: +1 703 830 2300
[email protected]
For editorial issues, like the status of your submitted paper or proposals, write to [email protected]
IOS Press
Nieuwe Hemweg 6B
1013 BG Amsterdam
The Netherlands
Tel: +31 20 688 3355
Fax: +31 20 687 0091
[email protected]
For editorial issues, permissions, book requests, submissions and proceedings, contact the Amsterdam office [email protected]
Inspirees International (China Office)
Ciyunsi Beili 207(CapitaLand), Bld 1, 7-901
100025, Beijing
China
Free service line: 400 661 8717
Fax: +86 10 8446 7947
[email protected]
For editorial issues, like the status of your submitted paper or proposals, write to [email protected]
如果您在出版方面需要帮助或有任何建, 件至: [email protected]