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
| Autor: | A. S. Kononikhin, Maria I. Indeykina, A. I. Spassky, K. V. Bocharov, Alexander A. Makarov, Sergey A. Kozin, Igor Popov, Yu. I. Kostyukevich, E. N. Nikolaev |
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| Rok vydání: | 2017 |
| Předmět: |
inorganic chemicals
0301 basic medicine 030102 biochemistry & molecular biology 010401 analytical chemistry Biophysics chemistry.chemical_element Zinc Mass spectrometry 01 natural sciences 0104 chemical sciences 03 medical and health sciences Deuterium Exchange Measurement chemistry Deuterium Structural Biology Ionization Physical chemistry Molecule Hydrogen–deuterium exchange Protein secondary structure |
| Zdroj: | Molecular Biology. 51:627-632 |
| ISSN: | 1608-3245 0026-8933 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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