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Mol Biol (Mosk). 2017 Jul-Aug;51(4):710-716. doi: 10.7868/S0026898417030107.

[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].

[Article in Russian]

Author information

Moscow Institute of Physics and Technology (State University), Dolgprudny, Moscow oblast, 141701 Russia.
Skolkovo Institute of Science and Technology, Skolkovo Innovation Center, Moscow, 143026 Russia.
Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, 119334 Russia.
Talrose Institute for Energy Problems of Chemical Physics, Russian Academy of Sciences, Moscow, 119334 Russia.
Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, 119991 Russia.


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.


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

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