Abstract
In this paper, 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–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 metal-binding sites. According to changes in NMR spectra, the manganese-binding center of the Aβ13-23 peptide is associated with the aspartate residue.
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Acknowledgments
Financial support was from the Russian government to support the Program of Competitive Growth of Kazan Federal University among the World’s Leading Academic Centers. This work was also funded by the subsidy allocated to the Kazan Federal University for the project part of the state assignment in the sphere of scientific activities (Center of Shared Facilities).
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Dmitriy Blokhin and Vladimir Klochkov contributed equally to this work.
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Abdrakhmanov, R., Blokhin, D., Usachev, K. et al. NMR Studies of the Mn2+ Interactions with Amyloid Peptide Aβ13-23 in Water Environment. BioNanoSci. 7, 204–206 (2017). https://doi.org/10.1007/s12668-016-0317-7
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DOI: https://doi.org/10.1007/s12668-016-0317-7