{"title":"Chameleonic Nature of Aβ: Implications for Alzheimer's and Other Amyloid Diseases","authors":"Birgit Strodel","doi":"10.1002/bies.70039","DOIUrl":null,"url":null,"abstract":"<p>The amyloid-<i>β</i> peptide (A<i>β</i>), implicated in Alzheimer's disease, exhibits significant polymorphism. At the monomer level, A<i>β</i> can adopt disordered, helical, and <i>β</i>-hairpin structures, influenced by environmental conditions. Both oligomeric and fibrillar states, characterized by the prevalence of <i>β</i>-sheets, are polymorphic in the arrangement of <i>β</i>-strands. This chameleon-like behavior arises from A<i>β</i>’s unique sequence and relatively flat energy landscape, which facilitates aggregation and may contribute to the prevalence of Alzheimer's disease, while also enabling disaggregation, thus slowing disease progression. In contrast, Creutzfeldt-Jakob disease, which is much rarer, progresses far more rapidly, likely due to the steeper energy landscape of the prion protein.</p>","PeriodicalId":9264,"journal":{"name":"BioEssays","volume":"47 9","pages":""},"PeriodicalIF":2.7000,"publicationDate":"2025-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/bies.70039","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"BioEssays","FirstCategoryId":"99","ListUrlMain":"https://onlinelibrary.wiley.com/doi/10.1002/bies.70039","RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
The amyloid-β peptide (Aβ), implicated in Alzheimer's disease, exhibits significant polymorphism. At the monomer level, Aβ can adopt disordered, helical, and β-hairpin structures, influenced by environmental conditions. Both oligomeric and fibrillar states, characterized by the prevalence of β-sheets, are polymorphic in the arrangement of β-strands. This chameleon-like behavior arises from Aβ’s unique sequence and relatively flat energy landscape, which facilitates aggregation and may contribute to the prevalence of Alzheimer's disease, while also enabling disaggregation, thus slowing disease progression. In contrast, Creutzfeldt-Jakob disease, which is much rarer, progresses far more rapidly, likely due to the steeper energy landscape of the prion protein.
期刊介绍:
molecular – cellular – biomedical – physiology – translational research – systems - hypotheses encouraged
BioEssays is a peer-reviewed, review-and-discussion journal. Our aims are to publish novel insights, forward-looking reviews and commentaries in contemporary biology with a molecular, genetic, cellular, or physiological dimension, and serve as a discussion forum for new ideas in these areas. An additional goal is to encourage transdisciplinarity and integrative biology in the context of organismal studies, systems approaches, through to ecosystems, where appropriate.