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

Secondary structure of Aβ(1–16) complexes with zinc: A study in the gas phase using... 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Molecular Biology Springer Journals

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

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Publisher
Pleiades Publishing
Copyright
Copyright © 2017 by Pleiades Publishing, Inc.
Subject
Life Sciences; Life Sciences, general; Biochemistry, general; Human Genetics
ISSN
0026-8933
eISSN
1608-3245
D.O.I.
10.1134/S0026893317030104
Publisher site
See Article on Publisher Site

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.

Journal

Molecular BiologySpringer Journals

Published: Aug 23, 2017

References

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