In this section
@article{Girvan:2016:10.1002/cbic.201600255,
author = {Girvan, P and Miyake, T and Teng, X and Branch, T and Ying, L},
doi = {10.1002/cbic.201600255},
journal = {Chembiochem},
pages = {1732--1737},
title = {Kinetics of the Interactions between Copper and Amyloid-β with FAD Mutations and Phosphorylation at the N-terminus},
url = {http://dx.doi.org/10.1002/cbic.201600255},
volume = {17},
year = {2016}
}
TY - JOUR
AB - Mutations and post-translational modifications of amyloid-β (Aβ) peptide in its Nterminus 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 serine8 (pS8). All three peptides bind to copper with a similar rate as the wild-type (wt). The dissociation rates follow the order pS8>H6R>wt>D7N; the interconversion between the two coordinating species occurs 50 % faster for H6R and pS8, whereas D7N had only a negligible effect. Interestingly, the rate of ternary complex (copper-bridged heterodimer) formation for the modified peptides was significantly faster than that for wt, thus leading us to propose that FAD and sporadic AD might share a kinetic origin for the enhanced oligomerisation of Aβ.
AU - Girvan,P
AU - Miyake,T
AU - Teng,X
AU - Branch,T
AU - Ying,L
DO - 10.1002/cbic.201600255
EP - 1737
PY - 2016///
SN - 1439-7633
SP - 1732
TI - Kinetics of the Interactions between Copper and Amyloid-β with FAD Mutations and Phosphorylation at the N-terminus
T2 - Chembiochem
UR - http://dx.doi.org/10.1002/cbic.201600255
UR - http://hdl.handle.net/10044/1/34045
VL - 17
ER -
