Biological and methodological complexities of beta‐amyloid peptide: Implications for Alzheimer’s disease research
| Autor: | Claire J. Garwood, Stephen B. Wharton, Julie E. Simpson, Martyna M. Matuszyk, Rosemary A. Staniforth, Laura Ferraiuolo |
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| Rok vydání: | 2021 |
| Předmět: |
Aged
80 and over chemistry.chemical_classification Amyloid beta-Peptides Disease onset Amyloid biology Amyloid beta Peptide Biochemistry Alzheimer's disease research Pathogenesis Cellular and Molecular Neuroscience chemistry Alzheimer Disease biology.protein Animals Humans Amyloid cascade Beta (finance) Neuroscience Aged |
| Zdroj: | Journal of Neurochemistry. 160:434-453 |
| ISSN: | 1471-4159 0022-3042 |
| Popis: | Although controversial, the amyloid cascade hypothesis remains central to the Alzheimer’s disease (AD) field and posits amyloid- beta (Aβ) as the central factor initiating disease onset. In recent years, there has been an increase in emphasis on studying the role of low molecular weight aggregates, such as oligomers, which are suggested to be more neurotoxic than fibrillary Aβ. Other Aβ isoforms, such as truncated Aβ, have also been implicated in disease. However, developing a clear understanding of AD pathogenesis has been hampered by the complexity of Aβ biochemistry in vitro and in vivo. This review explores factors contributing to the lack of consistency in experimental approaches taken to model Aβ aggregation and toxicity, and provides an overview of the different techniques available to analyse Aβ, such as electron and atomic force microscopy, nuclear magnetic resonance spectroscopy, dye-based assays, size exclusion chromatography, mass spectrometry, and SDS-PAGE. The review also explores how different types of Aβ can influence Aβ aggregation and toxicity, leading to variation in experimental outcomes, further highlighting the need for standardisation in Aβ preparations and methods used in current research. |
| Databáze: | OpenAIRE |
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