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β淀粉样肽 25-35 的构象和生物学活性。

Conformations and biological activities of amyloid beta peptide 25-35.

机构信息

Department of Molecular Biology, University of Siena, Italy.

出版信息

Curr Protein Pept Sci. 2010 Feb;11(1):54-67. doi: 10.2174/138920310790274626.


DOI:10.2174/138920310790274626
PMID:20201807
Abstract

Amyloid-beta (Abeta) peptide is commonly found in human Alzheimer's disease (AD) brain and is the main component of Alzheimer amyloid plaques. The predominant forms of Abeta in the human brain are Abeta(1-40) and Abeta(1-42), but Abeta(25-35) fragment, physiologically present in elderly people, is the more toxic region and has been recently found to play a relevant role in AD, due to its peculiar aggregation properties. In this work, we review the current understanding on the conformations and biological activity of Abeta(25-35) exploring aggregation, cytotoxic and neurodegenerative properties of this fundamental Abeta fragment, in order to provide an effective starting point to better approach a pathology spread and problematic as AD.

摘要

淀粉样肽-β(Abeta)在人类阿尔茨海默病(AD)脑中很常见,是阿尔茨海默淀粉样斑块的主要成分。人脑中的 Abeta 主要形式为 Abeta(1-40)和 Abeta(1-42),但生理上存在于老年人中的 Abeta(25-35)片段毒性更强,并且最近发现其在 AD 中起相关作用,这是由于其特殊的聚集特性。在这项工作中,我们回顾了对 Abeta(25-35)构象和生物学活性的现有认识,探索了该基本 Abeta 片段的聚集、细胞毒性和神经退行性特性,以期为更好地了解 AD 这样一种广泛传播和棘手的病理学提供一个有效的起点。

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