A Binuclear Zinc Interaction Fold Discovered in the Homodimer of Alzheimer's Amyloid-β Fragment with Taiwanese Mutation D7H

Polshakov V.I., Mantsyzov A.B., Kozin S.A., Adzhubei A.A., Zhokhov S.S., van Beek W., Kulikova A.A., Indeykina M.I., Mitkevich V.A., Makarov A.A.
Тип документаJournal Article
Дата публикации2017-09-18
Название журналаAngewandte Chemie - International Edition
ИздательWiley-Blackwell
Квартиль по SCImagoQ1
Квартиль по Web of ScienceQ1
Импакт-фактор 202116.82
ISSN14337851, 15213773
General Chemistry
Catalysis
Краткое описание
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.
Пристатейные ссылки: 21
Цитируется в публикациях: 18
Protein self-assembly via supramolecular strategies
Bai Y., Luo Q., Liu J.
Q1 Chemical Society Reviews 2016 цитирований: 145
Zinc(II) Binding Site to the Amyloid-β Peptide: Insights from Spectroscopic Studies with a Wide Series of Modified Peptides
Alies B., Conte-Daban A., Sayen S., Collin F., Kieffer I., Guillon E., Faller P., Hureau C.
Q1 Inorganic Chemistry 2016 цитирований: 57
Interplay of histidine residues of the Alzheimer's disease Aβ peptide governs its Zn-induced oligomerization
Istrate A.N., Kozin S.A., Zhokhov S.S., Mantsyzov A.B., Kechko O.I., Pastore A., Makarov A.A., Polshakov V.I.
Q1 Scientific Reports 2016 цитирований: 65
Open Access
Open access
Relationship between the architecture of zinc coordination and zinc binding affinity in proteins – insights into zinc regulation
Kochańczyk T., Drozd A., Krężel A.
Q1 Metallomics 2015 цитирований: 103
Peptide self-assembly triggered by metal ions
Zou R., Wang Q., Wu J., Wu J., Schmuck C., Tian H.
Q1 Chemical Society Reviews 2015 цитирований: 155
Amyloid β Protein and Alzheimer’s Disease: When Computer Simulations Complement Experimental Studies
Nasica-Labouze J., Nguyen P.H., Sterpone F., Berthoumieu O., Buchete N., Coté S., De Simone A., Doig A.J., Faller P., Garcia A., Laio A., Li M.S., Melchionna S., Mousseau N., Mu Y., et. al.
Q1 Chemical Reviews 2015 цитирований: 403
The English (H6R) familial Alzheimer's disease mutation facilitates zinc-induced dimerization of the amyloid-β metal-binding domain
Kozin S.A., Kulikova A.A., Istrate A.N., Tsvetkov P.O., Zhokhov S.S., Mezentsev Y.V., Kechko O.I., Ivanov A.S., Polshakov V.I., Makarov A.A.
Q1 Metallomics 2015 цитирований: 31
Disruption of zinc homeostasis and the pathogenesis of senile dementia
Kawahara M., Mizuno D., Koyama H., Konoha K., Ohkawara S., Sadakane Y.
Q1 Metallomics 2014 цитирований: 36
Phosphorylation of Ser8 promotes zinc-induced dimerization of the amyloid-β metal-binding domain
Kulikova A.A., Tsvetkov P.O., Indeykina M.I., Popov I.A., Zhokhov S.S., Golovin A.V., Polshakov V.I., Kozin S.A., Nudler E., Makarov A.A.
Q1 Molecular BioSystems 2014 цитирований: 39
Update on Zinc Biology
Solomons N.W.
Q2 Annals of Nutrition and Metabolism 2013 цитирований: 48
Amyloid-Beta (Aβ) D7H Mutation Increases Oligomeric Aβ42 and Alters Properties of Aβ-Zinc/Copper Assemblies
Chen W., Hong C., Lin Y., Chang W., Huang H., Liao J., Chang Y., Hsieh Y., Cheng C., Liu H., Chen Y., Cheng I.H.
Q1 PLoS ONE 2012 цитирований: 68
Open Access
Open access
NMR solution structure of rat Aβ(1-16): Toward understanding the mechanism of rats' resistance to Alzheimer's disease
Istrate A., Tsvetkov P., Mantsyzov A., Kulikova A., Kozin S., Makarov A., Polshakov V.
Q1 Biophysical Journal 2012 цитирований: 46
Open Access
Open access
Metalloproteomics
Permyakov E.A.
2009 цитирований: 29
Embryonic Neural Inducing Factor Churchill Is not a DNA-binding Zinc Finger Protein: Solution Structure Reveals a Solvent-exposed β-Sheet and Zinc Binuclear Cluster
Lee B.M., Buck-Koehntop B.A., Martinez-Yamout M.A., Dyson H.J., Wright P.E.
Q1 Journal of Molecular Biology 2007 цитирований: 14
Solution 1H NMR investigation of Zn2+ and Cd2+ binding to amyloid-beta peptide (Aβ) of Alzheimer's disease
Syme C.D., Viles J.H.
Q1 Biochimica et Biophysica Acta - Proteins and Proteomics 2006 цитирований: 127
Метрики
Поделиться
Цитировать
ГОСТ |
Цитировать
1. Polshakov V.I. и др. A Binuclear Zinc Interaction Fold Discovered in the Homodimer of Alzheimer’s Amyloid-β Fragment with Taiwanese Mutation D7H // Angewandte Chemie International Edition. 2017. Т. 56. № 39. С. 11734–11739.
RIS |
Цитировать

TY - JOUR

DO - 10.1002/anie.201704615

UR - http://dx.doi.org/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 - Kozin, Sergey A.

AU - Adzhubei, Alexei A.

AU - Zhokhov, Sergey S.

AU - van Beek, Wouter

AU - Kulikova, Alexandra A.

AU - Indeykina, Maria I.

AU - Mitkevich, Vladimir A.

AU - Makarov, Alexander A.

PY - 2017

DA - 2017/06/27

PB - Wiley

SP - 11734-11739

IS - 39

VL - 56

SN - 1433-7851

ER -

BibTex |
Цитировать

@article{2017,

doi = {10.1002/anie.201704615},

url = {https://doi.org/10.1002%2Fanie.201704615},

year = 2017,

month = {jun},

publisher = {Wiley},

volume = {56},

number = {39},

pages = {11734--11739},

author = {Vladimir I. Polshakov and Alexey B. Mantsyzov and Sergey A. Kozin and Alexei A. Adzhubei and Sergey S. Zhokhov and Wouter van{\hspace{0.25em}}Beek and Alexandra A. Kulikova and Maria I. Indeykina and Vladimir A. Mitkevich and Alexander A. Makarov},

title = {A Binuclear Zinc Interaction Fold Discovered in the Homodimer of Alzheimer{\textquotesingle}s Amyloid-$\upbeta$ Fragment with Taiwanese Mutation D7H}

}

MLA
Цитировать
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 56.39 (2017): 11734–11739. Crossref. Web.