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  • Berntsson, ElinaDepartment of Biochemistry and Biophysics, Arrhenius Laboratories, Stockholm University, Stockholm, Sweden; Department of Chemistry and Biotechnology, Tallinn University of Technology, Tallinn, Estonia (author)

Residue-specific binding of Ni(II) ions influences the structure and aggregation of amyloid beta (Aβ) peptides

  • Article/chapterEnglish2023

Publisher, publication year, extent ...

  • 2023-02-27
  • Nature Publishing Group,2023
  • electronicrdacarrier

Numbers

  • LIBRIS-ID:oai:DiVA.org:umu-205490
  • https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-205490URI
  • https://doi.org/10.1038/s41598-023-29901-5DOI
  • http://kipublications.ki.se/Default.aspx?queryparsed=id:152859195URI

Supplementary language notes

  • Language:English
  • Summary in:English

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  • Subject category:ref swepub-contenttype
  • Subject category:art swepub-publicationtype

Notes

  • 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.

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  • Vosough, FarazDepartment of Biochemistry and Biophysics, Arrhenius Laboratories, Stockholm University, Stockholm, Sweden (author)
  • Svantesson, TeodorDepartment of Biochemistry and Biophysics, Arrhenius Laboratories, Stockholm University, Stockholm, Sweden (author)
  • Pansieri, JonathanUmeå universitet,Institutionen för medicinsk kemi och biofysik(Swepub:umu)jopa0120 (author)
  • Iashchishyn, IgorUmeå universitet,Institutionen för medicinsk kemi och biofysik(Swepub:umu)igia0001 (author)
  • Ostojic, LucijaUmeå universitet,Institutionen för medicinsk kemi och biofysik(Swepub:umu)luos0004 (author)
  • Dong, XiaolinDepartment of Biochemistry and Biophysics, Arrhenius Laboratories, Stockholm University, Stockholm, Sweden (author)
  • Paul, SumanDepartment of Biochemistry and Biophysics, Arrhenius Laboratories, Stockholm University, Stockholm, Sweden (author)
  • Jarvet, JüriDepartment of Biochemistry and Biophysics, Arrhenius Laboratories, Stockholm University, Stockholm, Sweden; National Institute of Chemical Physics and Biophysics, Tallinn, Estonia (author)
  • Roos, Per M.Karolinska Institutet (author)
  • Barth, AndreasDepartment of Biochemistry and Biophysics, Arrhenius Laboratories, Stockholm University, Stockholm, Sweden (author)
  • Morozova-Roche, LudmillaUmeå universitet,Institutionen för medicinsk kemi och biofysik(Swepub:umu)lumo0001 (author)
  • Gräslund, AstridDepartment of Biochemistry and Biophysics, Arrhenius Laboratories, Stockholm University, Stockholm, Sweden (author)
  • Wärmländer, Sebastian K T SChemistry Section, Arrhenius Laboratories, Stockholm University, Stockholm, Sweden (author)
  • Department of Biochemistry and Biophysics, Arrhenius Laboratories, Stockholm University, Stockholm, Sweden; Department of Chemistry and Biotechnology, Tallinn University of Technology, Tallinn, EstoniaDepartment of Biochemistry and Biophysics, Arrhenius Laboratories, Stockholm University, Stockholm, Sweden (creator_code:org_t)

Related titles

  • In:Scientific Reports: Nature Publishing Group13:12045-2322

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