Zinc-induced interactions of the metal-binding domain of beta-amyloid with nucleic acids and glycosaminoglycans
- Авторы: Khmeleva S.A.1,2, Kozin S.A.1, Kiseleva Y.Y.2, Mitkevich V.A.1, Makarov A.A.1, Radko S.P.1,2
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Учреждения:
- Engelhardt Institute of Molecular Biology
- Orekhovich Institute of Biomedical Chemistry
- Выпуск: Том 50, № 6 (2016)
- Страницы: 927-929
- Раздел: Short Communications
- URL: https://journals.rcsi.science/0026-8933/article/view/162908
- DOI: https://doi.org/10.1134/S0026893316060091
- ID: 162908
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Аннотация
Zinc ions form complexes with β-amyloid peptides and play an important role in Alzheimer’s disease pathogenesis. It has been demonstrated by turbidimetry and correlation spectroscopy that synthetic peptide Aβ16 representing the metal-binding domain of β-amyloid is able to interact with nucleic acids, chondroitin polysulfate, and dextran sulfates in the presence of zinc ions. The amino acid D7H substitution enhanced the peptide binding to polyanions, whereas the H6R and H6A-H13A substitutions abolished this interaction. It is suggested that the metal-binding domain may serve as a zinc-dependent site of β-amyloid interaction with biological polyanions including DNA, RNA, and glycosaminoglycans.
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Об авторах
S. Khmeleva
Engelhardt Institute of Molecular Biology; Orekhovich Institute of Biomedical Chemistry
Email: radkos@yandex.ru
Россия, Moscow, 119991; Moscow, 119121
S. Kozin
Engelhardt Institute of Molecular Biology
Email: radkos@yandex.ru
Россия, Moscow, 119991
Y. Kiseleva
Orekhovich Institute of Biomedical Chemistry
Email: radkos@yandex.ru
Россия, Moscow, 119121
V. Mitkevich
Engelhardt Institute of Molecular Biology
Email: radkos@yandex.ru
Россия, Moscow, 119991
A. Makarov
Engelhardt Institute of Molecular Biology
Email: radkos@yandex.ru
Россия, Moscow, 119991
S. Radko
Engelhardt Institute of Molecular Biology; Orekhovich Institute of Biomedical Chemistry
Автор, ответственный за переписку.
Email: radkos@yandex.ru
Россия, Moscow, 119991; Moscow, 119121
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