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LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00005600naa a2200505 4500
001oai:DiVA.org:umu-205490
003SwePub
008230314s2023 | |||||||||||000 ||eng|
009oai:prod.swepub.kib.ki.se:152859195
0247 a https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-2054902 URI
0247 a https://doi.org/10.1038/s41598-023-29901-52 DOI
0247 a http://kipublications.ki.se/Default.aspx?queryparsed=id:1528591952 URI
040 a (SwePub)umud (SwePub)ki
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
1001 a Berntsson, Elinau Department of Biochemistry and Biophysics, Arrhenius Laboratories, Stockholm University, Stockholm, Sweden; Department of Chemistry and Biotechnology, Tallinn University of Technology, Tallinn, Estonia4 aut
2451 0a Residue-specific binding of Ni(II) ions influences the structure and aggregation of amyloid beta (Aβ) peptides
264 c 2023-02-27
264 1b Nature Publishing Group,c 2023
338 a electronic2 rdacarrier
520 a Alzheimer's disease (AD) is the most common cause of dementia worldwide. AD brains display deposits of insoluble amyloid plaques consisting mainly of aggregated amyloid-β (Aβ) peptides, and Aβ oligomers are likely a toxic species in AD pathology. AD patients display altered metal homeostasis, and AD plaques show elevated concentrations of metals such as Cu, Fe, and Zn. Yet, the metal chemistry in AD pathology remains unclear. Ni(II) ions are known to interact with Aβ peptides, but the nature and effects of such interactions are unknown. Here, we use numerous biophysical methods-mainly spectroscopy and imaging techniques-to characterize Aβ/Ni(II) interactions in vitro, for different Aβ variants: Aβ(1-40), Aβ(1-40)(H6A, H13A, H14A), Aβ(4-40), and Aβ(1-42). We show for the first time that Ni(II) ions display specific binding to the N-terminal segment of full-length Aβ monomers. Equimolar amounts of Ni(II) ions retard Aβ aggregation and direct it towards non-structured aggregates. The His6, His13, and His14 residues are implicated as binding ligands, and the Ni(II)·Aβ binding affinity is in the low µM range. The redox-active Ni(II) ions induce formation of dityrosine cross-links via redox chemistry, thereby creating covalent Aβ dimers. In aqueous buffer Ni(II) ions promote formation of beta sheet structure in Aβ monomers, while in a membrane-mimicking environment (SDS micelles) coil-coil helix interactions appear to be induced. For SDS-stabilized Aβ oligomers, Ni(II) ions direct the oligomers towards larger sizes and more diverse (heterogeneous) populations. All of these structural rearrangements may be relevant for the Aβ aggregation processes that are involved in AD brain pathology.
650 7a NATURVETENSKAPx Biologix Strukturbiologi0 (SwePub)106012 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciencesx Structural Biology0 (SwePub)106012 hsv//eng
7001 a Vosough, Farazu Department of Biochemistry and Biophysics, Arrhenius Laboratories, Stockholm University, Stockholm, Sweden4 aut
7001 a Svantesson, Teodoru Department of Biochemistry and Biophysics, Arrhenius Laboratories, Stockholm University, Stockholm, Sweden4 aut
7001 a Pansieri, Jonathanu Umeå universitet,Institutionen för medicinsk kemi och biofysik4 aut0 (Swepub:umu)jopa0120
7001 a Iashchishyn, Igoru Umeå universitet,Institutionen för medicinsk kemi och biofysik4 aut0 (Swepub:umu)igia0001
7001 a Ostojic, Lucijau Umeå universitet,Institutionen för medicinsk kemi och biofysik4 aut0 (Swepub:umu)luos0004
7001 a Dong, Xiaolinu Department of Biochemistry and Biophysics, Arrhenius Laboratories, Stockholm University, Stockholm, Sweden4 aut
7001 a Paul, Sumanu Department of Biochemistry and Biophysics, Arrhenius Laboratories, Stockholm University, Stockholm, Sweden4 aut
7001 a Jarvet, Jüriu Department of Biochemistry and Biophysics, Arrhenius Laboratories, Stockholm University, Stockholm, Sweden; National Institute of Chemical Physics and Biophysics, Tallinn, Estonia4 aut
7001 a Roos, Per M.u Karolinska Institutet4 aut
7001 a Barth, Andreasu Department of Biochemistry and Biophysics, Arrhenius Laboratories, Stockholm University, Stockholm, Sweden4 aut
7001 a Morozova-Roche, Ludmillau Umeå universitet,Institutionen för medicinsk kemi och biofysik4 aut0 (Swepub:umu)lumo0001
7001 a Gräslund, Astridu Department of Biochemistry and Biophysics, Arrhenius Laboratories, Stockholm University, Stockholm, Sweden4 aut
7001 a Wärmländer, Sebastian K T Su Chemistry Section, Arrhenius Laboratories, Stockholm University, Stockholm, Sweden4 aut
7102 a Department of Biochemistry and Biophysics, Arrhenius Laboratories, Stockholm University, Stockholm, Sweden; Department of Chemistry and Biotechnology, Tallinn University of Technology, Tallinn, Estoniab Department of Biochemistry and Biophysics, Arrhenius Laboratories, Stockholm University, Stockholm, Sweden4 org
7730 t Scientific Reportsd : Nature Publishing Groupg 13:1q 13:1x 2045-2322
8564 u https://doi.org/10.1038/s41598-023-29901-5y Fulltext
8564 u https://umu.diva-portal.org/smash/get/diva2:1743241/FULLTEXT01.pdfx primaryx Raw objecty fulltext:print
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-205490
8564 8u https://doi.org/10.1038/s41598-023-29901-5
8564 8u http://kipublications.ki.se/Default.aspx?queryparsed=id:152859195

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