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Phosphorylation of Full Length Amyloid-β Peptide Modulates its Amyloid Aggregation, Cell Binding and Neurotoxic Properties

Abstract

Amyloid beta peptide (Aβ) is the major protein component of the amyloid plaques that are present in brains of Alzheimer’s disease (AD) patients. Aβ42 peptide is a known neurotoxic agent that binds to neurons and under specific aggregation conditions to trigger the cells death. Aβ peptide can undergo specific amino acid posttranslational modifications such as phosphorylation that are important for modulating its proteolytic degradation, aggregation, binding to lipid membranes and neurotoxic functions. Peptides phosphorylated at serine 8 in the full length Aβ42 (pAβ42) were synthesised and compared to native Aβ42 peptide. Their secondary structures, aggregation properties and interaction with plasma membranes of primary cortical neurons investigated. The results revealed that pAβ42 had increased β-sheet formation with rapid amyloid formation in a synthetic lipid environment which was associated with increased cellular binding but concomitant diminished neurotoxicity. Our data support the notion that phosphorylation of Aβ42 promotes formation of amyloid plaques in the brain which lack the neurotoxic properties associated with oligomeric species causing the pathogenesis in AD.

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Publication details

The article was received on 27 Apr 2017, accepted on 29 May 2017 and first published on 01 Jun 2017


Article type: Paper
DOI: 10.1039/C7MB00249A
Citation: Mol. BioSyst., 2017, Accepted Manuscript
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    Phosphorylation of Full Length Amyloid-β Peptide Modulates its Amyloid Aggregation, Cell Binding and Neurotoxic Properties

    E. Jamasbi, F. Separovic, A. Hossain and G. D. Ciccotosto, Mol. BioSyst., 2017, Accepted Manuscript , DOI: 10.1039/C7MB00249A

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