Amyloid-β (Aβ) peptide is commonly found in human Alzheimer's 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.

Millucci, L., Ghezzi, L., Bernardini, G., & Santucci, A. (2010). Conformations and biological activities of Amyloid Beta Peptide 25-35. CURRENT PROTEIN & PEPTIDE SCIENCE, 11(1), 54-67 [10.2174/138920310790274626].

Conformations and biological activities of Amyloid Beta Peptide 25-35

MILLUCCI, LIA;GHEZZI, LORENZO;BERNARDINI, GIULIA;SANTUCCI, ANNALISA
2010

Abstract

Amyloid-β (Aβ) peptide is commonly found in human Alzheimer's 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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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11365/20839
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