Kazan (Volga region) Federal University, KFU
KAZAN
FEDERAL UNIVERSITY
 
NMR STUDIES OF THE MN2+ INTERACTIONS WITH AMYLOID PEPTIDE Aβ13-23 IN WATER ENVIRONMENT
Form of presentationArticles in international journals and collections
Year of publication2016
  • Karataeva Farida Khaydarovna, author
  • Klochkov Vladimir Vasilevich, author
  • Usachev Konstantin Sergeevich, author
  • Abdrakhmanov Rustam Zhamilevich, postgraduate kfu
  • Bibliographic description in the original language Binding of Mn2+ ions to the fragment of beta-amyloid peptide (Aβ13-23) was studied. Manganese complexation induces important structural changes within the C-terminal segment of the peptide. Investigation of peptide Ab metal ion binding was made by MnCl2 salt titration and recording 2D 1H-1H NMR TOCSY spectra (TOtal Correlation SpectroscopY). Multidimensional NMR techniques were performed to understand the details of the conformational behavior of the peptide and to reveal the metalbinding sites. According to changes in NMR spectra, the manganese-binding center of the Aβ13-23 peptide is associated with the aspartate residue.
    Keywords Amyloid peptide Aβ13-23, NMR spectroscopy, Mn2+ ions
    The name of the journal BioNanoScience
    Please use this ID to quote from or refer to the card https://repository.kpfu.ru/eng/?p_id=148699&p_lang=2

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