Zinc-induced interactions of the metal-binding domain of beta-amyloid with nucleic acids and glycosaminoglycans
- Авторлар: 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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Мекемелер:
- Engelhardt Institute of Molecular Biology
- Orekhovich Institute of Biomedical Chemistry
- Шығарылым: Том 50, № 6 (2016)
- Беттер: 927-929
- Бөлім: Short Communications
- URL: https://journal-vniispk.ru/0026-8933/article/view/162908
- DOI: https://doi.org/10.1134/S0026893316060091
- ID: 162908
Дәйексөз келтіру
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.
Негізгі сөздер
Авторлар туралы
S. Khmeleva
Engelhardt Institute of Molecular Biology; Orekhovich Institute of Biomedical Chemistry
Email: radkos@yandex.ru
Ресей, Moscow, 119991; Moscow, 119121
S. Kozin
Engelhardt Institute of Molecular Biology
Email: radkos@yandex.ru
Ресей, Moscow, 119991
Y. Kiseleva
Orekhovich Institute of Biomedical Chemistry
Email: radkos@yandex.ru
Ресей, Moscow, 119121
V. Mitkevich
Engelhardt Institute of Molecular Biology
Email: radkos@yandex.ru
Ресей, Moscow, 119991
A. Makarov
Engelhardt Institute of Molecular Biology
Email: radkos@yandex.ru
Ресей, Moscow, 119991
S. Radko
Engelhardt Institute of Molecular Biology; Orekhovich Institute of Biomedical Chemistry
Хат алмасуға жауапты Автор.
Email: radkos@yandex.ru
Ресей, Moscow, 119991; Moscow, 119121
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