Based on molecular structures: Amyloid-β generation, clearance, toxicity and therapeutic strategies

Amyloid-β (Aβ) has long been considered as one of the most important pathogenic factors in Alzheimer’s disease (AD), but the specific pathogenic mechanism of Aβ is still not completely understood. In recent years, the development of structural biology technology has led to new understandings about A...

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Published inFrontiers in molecular neuroscience Vol. 15; p. 927530
Main Authors Yang, Hai, Li, Jinping, Li, Xiaoxiong, Ma, Linqiu, Hou, Mingliang, Zhou, Huadong, Zhou, Rui
Format Journal Article
LanguageEnglish
Published Lausanne Frontiers Research Foundation 31.08.2022
Frontiers Media S.A
Subjects
Alzheimer's disease
amyloid-β
Dementia
Metabolism
Molecular structure
Neurodegenerative diseases
Neuroscience
NMR
Nuclear magnetic resonance
Peptides
therapeutic strategies
Toxicity
β-Amyloid
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Summary:Amyloid-β (Aβ) has long been considered as one of the most important pathogenic factors in Alzheimer’s disease (AD), but the specific pathogenic mechanism of Aβ is still not completely understood. In recent years, the development of structural biology technology has led to new understandings about Aβ molecular structures, Aβ generation and clearance from the brain and peripheral tissues, and its pathological toxicity. The purpose of the review is to discuss Aβ metabolism and toxicity, and the therapeutic strategy of AD based on the latest progress in molecular structures of Aβ. The Aβ structure at the atomic level has been analyzed, which provides a new and refined perspective to comprehend the role of Aβ in AD and to formulate therapeutic strategies of AD.
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These authors have contributed equally to this work
This article was submitted to Brain Disease Mechanisms, a section of the journal Frontiers in Molecular Neuroscience
Edited by: Mohammad Haddadi, University of Zabol, Iran
Reviewed by: Homira Behbahani, Karolinska Institutet (KI), Sweden; Kazumasa Saigoh, Kindai University Hospital, Japan
ISSN:1662-5099
1662-5099
DOI:10.3389/fnmol.2022.927530