Evaluation of Cu(i) binding to the E2 domain of the amyloid precursor protein – a lesson in quantification of metal binding to proteinsvialigand competition-Reference-Cited by-同舟云学术

Evaluation of Cu(i) binding to the E2 domain of the amyloid precursor protein – a lesson in quantification of metal binding to proteinsvialigand competition

Published:2018 Issue:1 Volume:10 Page:108-119
ISSN:1756-5901
Container-title:Metallomics
language:en
Short-container-title:Metallomics

Author:

Young Tessa R.¹²³⁴^ORCID,Wedd Anthony G.¹²³⁴,Xiao Zhiguang¹²³⁴⁵^ORCID

Affiliation:

1. School of Chemistry and Bio21 Molecular Science and Biotechnology Institute

2. The University of Melbourne

3. Parkville

4. Australia

5. Melbourne Dementia Research Centre

Abstract

APP E2 forms stable Cu(i)-mediated ternary complexes with several competing ligands, but not upon addition of heparin. This allows a systematic review of general conditions for quantification of metal–protein affinity and new insights into the physiological functions of APP.

Funder

Australian Research Council

Publisher

Oxford University Press (OUP)

Subject

Metals and Alloys,Biochemistry,Biomaterials,Biophysics,Chemistry (miscellaneous)

Link

http://pubs.rsc.org/en/content/articlepdf/2018/MT/C7MT00291B

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