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Article

Kinetics of the Interactions between Copper and Amyloid-β with FAD Mutations and Phosphorylation at the N terminus.

Chembiochem : a European journal of chemical biology - 15 Sept 2016

Girvan Paul, Miyake Toru, Teng Xiangyu, Branch Thomas, Ying Liming

Abstract excerpt

Mutations and post-translational modifications of amyloid-β (Aβ) peptide in its N terminus have been shown to increase fibril formation, yet the molecular mechanism is not clear. Here we investigated the kinetics of the interactions of copper with two Aβ peptides containing Familial Alzheimer's disease (FAD) mutations (English (H6R) and Tottori (D7N)), as well as with Aβ peptide phosphorylated at serine 8 (pS8)....

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Identifiers

PMID: 27356100
DOI: 10.1002/cbic.201600255
PMCID: PMC5096041

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