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Peer-reviewedCC BY-NC-ND 4.0Communications Chemistry

Soluble zinc-induced amyloid β oligomers probed through fluorine NMR spectroscopy

  • Luigi Russo1
  • Kalyan S. Chakrabarti2
  • Robin Backer3
  • Kerstin Overkamp4
  • Serge Gambarelli5
  • Dieter Willbold3,6
  • Giuseppe Sicoli7
  • Nasrollah Rezaei-Ghaleh8
8 affiliations
  1. 1Department of Environmental, Biological and Pharmaceutical Science and Technology, University of Campania Luigi Vanvitelli, Caserta, Italy
  2. 2Department of Biological Science and Chemistry, Krea University, Sri city, Andhra Pradesh India
  3. 3Institute of Physical Biology, Heinrich Heine University Düsseldorf, Universitätsstraße 1, Düsseldorf, Germany
  4. 4Department of NMR-based Structural Biology, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany
  5. 5Univ. Grenoble Alpes, CEA, CNRS, IRIG, SyMMES, Grenoble, France
  6. 6Institute of Biological Information Processing, IBI-7: Structural Biochemistry, Forschungszentrum Jülich, Jülich, Germany
  7. 7CNRS UMR 8516, University of Lille, Villeneuve d’Ascq, France
  8. 8Department of Molecular Medicine, University of Pavia, Pavia, Italy
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Abstract

Divalent zinc ions (Zn) interact with amyloid β (Aβ) peptides and influence its Alzheimer disease (AD)-related aggregation. Little is known about the structural properties of Zn-induced Aβ oligomers. Here, we report recombinant production of fluorinated Aβ40 at Phe4, Tyr10, Phe19 and Phe20 residues and utilize these fluorinated residues as proxies to interrogate Zn-induced Aβ40 oligomers. Our NMR and CW EPR results confirm Zn binding to the N-terminal region of Aβ40 and demonstrate the reversible oligomerization and irreversible aggregation of Aβ40 upon Zn addition. The 19F NMR relaxation and dark-state exchange saturation transfer (DEST) data provide dynamical information on free Aβ40 and demonstrate that monomeric Aβ40 is in exchange with small Zn-induced Aβ40 oligomers with less than about 60 kDa molecular weight on a millisecond timescale. The 19F ENDOR data suggest that the distance between the N-terminally attached nitroxide spin and fluorinated residues within the Zn-Aβ40 aggregates is larger than about 1.5 nm. Our results shed light on the properties of soluble Zn-induced Aβ oligomers and pave the way for further structural characterization of these Aβ aggregates.

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Cite

BibTeXRIS
BibTeX
@article{russo2026soluble,
  title = {{Soluble zinc-induced amyloid β oligomers probed through fluorine NMR spectroscopy}},
  author = {Luigi Russo and Kalyan S. Chakrabarti and Robin Backer and Kerstin Overkamp and Serge Gambarelli and Dieter Willbold and Giuseppe Sicoli and Nasrollah Rezaei-Ghaleh},
  journal = {Communications Chemistry},
  year = {2026},
  month = jul,
  doi = {10.1038/s42004-026-02121-4},
  url = {https://doi.org/10.1038/s42004-026-02121-4},
  note = {CC BY-NC-ND 4.0},
}
RIS
TY  - JOUR
TI  - Soluble zinc-induced amyloid β oligomers probed through fluorine NMR spectroscopy
AU  - Luigi Russo
AU  - Kalyan S. Chakrabarti
AU  - Robin Backer
AU  - Kerstin Overkamp
AU  - Serge Gambarelli
AU  - Dieter Willbold
AU  - Giuseppe Sicoli
AU  - Nasrollah Rezaei-Ghaleh
PY  - 2026
DA  - 2026/07/13
JO  - Communications Chemistry
DO  - 10.1038/s42004-026-02121-4
UR  - https://doi.org/10.1038/s42004-026-02121-4
AB  - Divalent zinc ions (Zn) interact with amyloid β (Aβ) peptides and influence its Alzheimer disease (AD)-related aggregation. Little is known about the structural properties of Zn-induced Aβ oligomers. Here, we report recombinant production of fluorinated Aβ40 at Phe4, Tyr10, Phe19 and Phe20 residues and utilize these fluorinated residues as proxies to interrogate Zn-induced Aβ40 oligomers. Our NMR and CW EPR results confirm Zn binding to the N-terminal region of Aβ40 and demonstrate the reversible oligomerization and irreversible aggregation of Aβ40 upon Zn addition. The 19F NMR relaxation and dark-state exchange saturation transfer (DEST) data provide dynamical information on free Aβ40 and demonstrate that monomeric Aβ40 is in exchange with small Zn-induced Aβ40 oligomers with less than about 60 kDa molecular weight on a millisecond timescale. The 19F ENDOR data suggest that the distance between the N-terminally attached nitroxide spin and fluorinated residues within the Zn-Aβ40 aggregates is larger than about 1.5 nm. Our results shed light on the properties of soluble Zn-induced Aβ oligomers and pave the way for further structural characterization of these Aβ aggregates.
SN  - 2399-3669
ER  -