Abstract
Amyloid-β (Aβ) peptide is commonly found in human Alzheimers disease (AD) brain and is the main component of Alzheimer amyloid plaques. The predominant forms of Aβ in the human brain are Aβ(1-40) and Aβ(1-42), but Aβ(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 Aβ(25-35) exploring aggregation, cytotoxic and neurodegenerative properties of this fundamental Aβ fragment, in order to provide an effective starting point to better approach a pathology spread and problematic as AD.
Keywords: Aβ(25-35), Alzheimer's disease, aggregation, amyloid, neurotoxicity, structure analysis
Current Protein & Peptide Science
Title: Conformations and Biological Activities of Amyloid Beta Peptide 25-35
Volume: 11 Issue: 1
Author(s): L. Millucci, L. Ghezzi, G. Bernardini and A. Santucci
Affiliation:
Keywords: Aβ(25-35), Alzheimer's disease, aggregation, amyloid, neurotoxicity, structure analysis
Abstract: Amyloid-β (Aβ) peptide is commonly found in human Alzheimers disease (AD) brain and is the main component of Alzheimer amyloid plaques. The predominant forms of Aβ in the human brain are Aβ(1-40) and Aβ(1-42), but Aβ(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 Aβ(25-35) exploring aggregation, cytotoxic and neurodegenerative properties of this fundamental Aβ fragment, in order to provide an effective starting point to better approach a pathology spread and problematic as AD.
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Cite this article as:
Millucci L., Ghezzi L., Bernardini G. and Santucci A., Conformations and Biological Activities of Amyloid Beta Peptide 25-35, Current Protein & Peptide Science 2010; 11 (1) . https://dx.doi.org/10.2174/138920310790274626
DOI https://dx.doi.org/10.2174/138920310790274626 |
Print ISSN 1389-2037 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5550 |
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