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A binuclear zinc interaction fold discovered in homodimer of Alzheimer's amyloid-beta fragment with Taiwanese mutation D7Hстатья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 19 октября 2017 г.
- Авторы: 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.
- Журнал: Angewandte Chemie - International Edition
- Том: 56
- Номер: 39
- Год издания: 2017
- Издательство: John Wiley & Sons Ltd.
- Местоположение издательства: United Kingdom
- Первая страница: 11734
- Последняя страница: 11739
- DOI: 10.1002/anie.201704615
- Аннотация: Zinc induced oligomerization of amyloid-beta peptide (Abeta) produces potentially pathogenic agents of Alzheimer’s disease. Earlier we showed that mutations and modifications in the metal binding domain 1-16 of Abeta peptide crucially affected its zinc induced oligomerization by changing intermolecular zinc mediated interface. 3D structure of this interface appearing in a range of Abeta species is important since it represents a prospective drug target for disease modifying therapy. Using NMR spectroscopy, EXAFS spectroscopy, mass spectrometry and isothermal titration calorimetry we have studied interaction of zinc ions with Abeta fragments 1-7 and 1-10 carrying familial Taiwanese mutation D7H. 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. Novel binuclear zinc interaction fold in the dimer structure has been discovered. It can be used for designing zinc regulated proteins and zinc mediated self-assembling peptides.
- Добавил в систему: Манцызов Алексей Борисович