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

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• 作者：S. A. Khmeleva ; S. A. Kozin ; Y. Y. Kiseleva ; V. A. Mitkevich…
• 关键词：Alzheimer disease ; beta ; amyloid ; zinc ; nucleic acids ; glycosaminoglycans
• 刊名：Molecular Biology
• 出版年：2016
• 出版时间：November 2016
• 年：2016
• 卷：50
• 期：6
• 页码：927-929
• 全文大小：
• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Life Sciences, general; Biochemistry, general; Human Genetics;
• 出版者：Pleiades Publishing
• ISSN：1608-3245
• 卷排序：50

文摘

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.