Zinc-induced interactions of the metal-binding domain of beta-amyloid with nucleic acids and glycosaminoglycans
- 作者: 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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隶属关系:
- Engelhardt Institute of Molecular Biology
- Orekhovich Institute of Biomedical Chemistry
- 期: 卷 50, 编号 6 (2016)
- 页面: 927-929
- 栏目: Short Communications
- URL: https://journal-vniispk.ru/0026-8933/article/view/162908
- DOI: https://doi.org/10.1134/S0026893316060091
- ID: 162908
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详细
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.
作者简介
S. Khmeleva
Engelhardt Institute of Molecular Biology; Orekhovich Institute of Biomedical Chemistry
Email: radkos@yandex.ru
俄罗斯联邦, Moscow, 119991; Moscow, 119121
S. Kozin
Engelhardt Institute of Molecular Biology
Email: radkos@yandex.ru
俄罗斯联邦, Moscow, 119991
Y. Kiseleva
Orekhovich Institute of Biomedical Chemistry
Email: radkos@yandex.ru
俄罗斯联邦, Moscow, 119121
V. Mitkevich
Engelhardt Institute of Molecular Biology
Email: radkos@yandex.ru
俄罗斯联邦, Moscow, 119991
A. Makarov
Engelhardt Institute of Molecular Biology
Email: radkos@yandex.ru
俄罗斯联邦, Moscow, 119991
S. Radko
Engelhardt Institute of Molecular Biology; Orekhovich Institute of Biomedical Chemistry
编辑信件的主要联系方式.
Email: radkos@yandex.ru
俄罗斯联邦, Moscow, 119991; Moscow, 119121
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