Journal article

Phosphorylation of a full length amyloid-beta peptide modulates its amyloid aggregation, cell binding and neurotoxic properties

Elaheh Jamasbi, Frances Separovic, Mohammed Akhter Hossain, Giuseppe Donato Ciccotosto

MOLECULAR BIOSYSTEMS | ROYAL SOC CHEMISTRY | Published : 2017

Abstract

Amyloid beta peptide (Aβ) is the major protein component of the amyloid plaques that are present in the brains of Alzheimer's disease (AD) patients. Aβ42 peptide is a known neurotoxic agent that binds to neurons and, under specific aggregation conditions, triggers cell 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 full-length Aβ42 (pAβ42) were synthesised and compared to native Aβ42 peptide. Their secondary structures, aggregation properties and interactions with pl..

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