A Binuclear Zinc Interaction Fold Discovered in the Homodimer of Alzheimer's Amyloid-β Fragment with Taiwanese Mutation D7H
Vladimir I. Polshakov
1, 2, 3, 4
,
Alexey B. Mantsyzov
2, 4
,
С. А. Козин
1, 3
,
Alexei Adzhubei
1, 3
,
Sergey S Zhokhov
2, 4
,
Wouter van Beek
5, 6
,
Alexandra A Kulikova
1, 3
,
Maria I Indeykina
7, 8
,
В. А. Митькевич
1, 3
,
Alexander A. Makarov
1, 3
Publication type: Journal Article
Publication date: 2017-06-27
scimago Q1
wos Q1
SJR: 5.550
CiteScore: 27.6
Impact factor: 16.9
ISSN: 14337851, 15213773
PubMed ID:
28570778
General Chemistry
Catalysis
Abstract
Zinc‐induced oligomerization of amyloid‐β peptide (Aβ) produces potentially pathogenic agents of Alzheimer's disease. Mutations and modifications in the metal binding domain 1–16 of Aβ peptide crucially affect its zinc‐induced oligomerization by changing intermolecular zinc mediated interface. The 3D structure of this interface appearing in a range of Aβ species is a prospective drug target for disease modifying therapy. Using NMR spectroscopy, EXAFS spectroscopy, mass spectrometry, and isothermal titration calorimetry the interaction of zinc ions with Aβ fragments 1–7 and 1–10 carrying familial Taiwanese mutation D7H was studied. Zinc ions induce formation of a stable homodimer formed by the two peptide chains fastened by two zinc ions and stacking interactions of imidazole rings. A binuclear zinc interaction fold in the dimer structure was discovered. It can be used for designing zinc‐regulated proteins and zinc‐mediated self‐assembling peptides.
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27
Total citations:
27
Citations from 2024:
7
(25%)
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GOST
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Polshakov V. I. et al. A Binuclear Zinc Interaction Fold Discovered in the Homodimer of Alzheimer's Amyloid-β Fragment with Taiwanese Mutation D7H // Angewandte Chemie - International Edition. 2017. Vol. 56. No. 39. pp. 11734-11739.
GOST all authors (up to 50)
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Polshakov V. I., Mantsyzov A. B., Козин С. А., Adzhubei A., Zhokhov S. S., van Beek W., Kulikova A. A., Indeykina M. I., Митькевич В. А., Makarov A. A. A Binuclear Zinc Interaction Fold Discovered in the Homodimer of Alzheimer's Amyloid-β Fragment with Taiwanese Mutation D7H // Angewandte Chemie - International Edition. 2017. Vol. 56. No. 39. pp. 11734-11739.
Cite this
RIS
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TY - JOUR
DO - 10.1002/anie.201704615
UR - https://onlinelibrary.wiley.com/doi/10.1002/anie.201704615
TI - A Binuclear Zinc Interaction Fold Discovered in the Homodimer of Alzheimer's Amyloid-β Fragment with Taiwanese Mutation D7H
T2 - Angewandte Chemie - International Edition
AU - Polshakov, Vladimir I.
AU - Mantsyzov, Alexey B.
AU - Козин, С. А.
AU - Adzhubei, Alexei
AU - Zhokhov, Sergey S
AU - van Beek, Wouter
AU - Kulikova, Alexandra A
AU - Indeykina, Maria I
AU - Митькевич, В. А.
AU - Makarov, Alexander A.
PY - 2017
DA - 2017/06/27
PB - Wiley
SP - 11734-11739
IS - 39
VL - 56
PMID - 28570778
SN - 1433-7851
SN - 1521-3773
ER -
Cite this
BibTex (up to 50 authors)
Copy
@article{2017_Polshakov,
author = {Vladimir I. Polshakov and Alexey B. Mantsyzov and С. А. Козин and Alexei Adzhubei and Sergey S Zhokhov and Wouter van Beek and Alexandra A Kulikova and Maria I Indeykina and В. А. Митькевич and Alexander A. Makarov},
title = {A Binuclear Zinc Interaction Fold Discovered in the Homodimer of Alzheimer's Amyloid-β Fragment with Taiwanese Mutation D7H},
journal = {Angewandte Chemie - International Edition},
year = {2017},
volume = {56},
publisher = {Wiley},
month = {jun},
url = {https://onlinelibrary.wiley.com/doi/10.1002/anie.201704615},
number = {39},
pages = {11734--11739},
doi = {10.1002/anie.201704615}
}
Cite this
MLA
Copy
Polshakov, Vladimir I., et al. “A Binuclear Zinc Interaction Fold Discovered in the Homodimer of Alzheimer's Amyloid-β Fragment with Taiwanese Mutation D7H.” Angewandte Chemie - International Edition, vol. 56, no. 39, Jun. 2017, pp. 11734-11739. https://onlinelibrary.wiley.com/doi/10.1002/anie.201704615.