Secondary structure of Aβ(1–16) complexes with zinc: A study in the gas phase using deuterium/hydrogen exchange and ultra-high-resolution mass spectrometry

Yu I. Kostyukevich, A. S. Kononikhin, M. I. Indeykina, I. A. Popov, K. V. Bocharov, A. I. Spassky, S. A. Kozin, A. A. Makarov, E. N. Nikolaev

    Research output: Contribution to journalArticlepeer-review

    Abstract

    Complexes of peptide fragment 1–16 of beta-amyloid with transition metals play an important role in the development of a broad class of neurodegenerative diseases, which determines the interest in investigating the structures of these complexes. In this work, we have applied the method of the deuterium/hydrogen exchange in combination with ultra-high-resolution mass spectrometry to study conformational changes in (1–16) beta-amyloid peptide induced by binding of zinc(II) atoms. The efficiency of the deuterium/hydrogen exchange depended on the number of zinc atoms bound to the peptide and on the temperature of the ionization source region. Deuterium/hydrogen exchange reactions have been performed directly in the ionization source. The number of exchanges decreased considerably with an increasing numbers of zinc atoms. The relationship has been described with a damped exponential curve, which indicated that the binding of zinc atoms altered the conformation of the peptide ion by making it less open, which limits the access to inner areas of the molecule.

    Original languageEnglish
    Pages (from-to)627-632
    Number of pages6
    JournalMolecular Biology
    Volume51
    Issue number4
    DOIs
    Publication statusPublished - 1 Jul 2017

    Keywords

    • beta-amyloid
    • deuterium/hydrogen exchange
    • electrospray
    • mass spectrometry
    • secondary structure

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