Zinc-induced interactions of the metal-binding domain of beta-amyloid with nucleic acids and glycosaminoglycans


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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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