Angewandte Chemie - International Edition, volume 56, issue 39, pages 11734-11739
A Binuclear Zinc Interaction Fold Discovered in the Homodimer of Alzheimer's Amyloid-β Fragment with Taiwanese Mutation D7H
Polshakov Vladimir I.
1, 2
,
Козин С. А.
1
,
Adzhubei Alexei
1
,
Zhokhov Sergey S
2
,
van Beek Wouter
3
,
Indeykina Maria I
4
,
Митькевич В. А.
1
,
Makarov Alexander A.
1
Publication type: Journal Article
Publication date: 2017-06-27
Quartile SCImago
Q1
Quartile WOS
Q1
Impact factor: 16.6
ISSN: 14337851, 15213773
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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- We do not take into account publications that without a DOI.
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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.
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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.
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TY - JOUR
DO - 10.1002/anie.201704615
UR - https://doi.org/10.1002%2Fanie.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 - van Beek, Wouter
AU - Indeykina, Maria I
AU - Makarov, Alexander A.
AU - Polshakov, Vladimir I.
AU - Mantsyzov, Alexey B.
AU - Козин, С. А.
AU - Adzhubei, Alexei
AU - Zhokhov, Sergey S
AU - Kulikova, Alexandra A
AU - Митькевич, В. А.
PY - 2017
DA - 2017/06/27 00:00:00
PB - Wiley
SP - 11734-11739
IS - 39
VL - 56
SN - 1433-7851
SN - 1521-3773
ER -
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@article{2017_Polshakov,
author = {Wouter van Beek and Maria I Indeykina and Alexander A. Makarov and Vladimir I. Polshakov and Alexey B. Mantsyzov and С. А. Козин and Alexei Adzhubei and Sergey S Zhokhov and Alexandra A Kulikova and В. А. Митькевич},
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://doi.org/10.1002%2Fanie.201704615},
number = {39},
pages = {11734--11739},
doi = {10.1002/anie.201704615}
}
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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://doi.org/10.1002%2Fanie.201704615.