NDLI: Evaluation of quantitative probes for weaker Cu(i) binding sites completes a set of four capable of detecting Cu(i) affinities from nanomolar to attomolar

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Metallomics Vol - 5 Issue - 4

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Evaluation of quantitative probes for weaker Cu(i) binding sites completes a set of four capable of detecting Cu(i) affinities from nanomolar to attomolar

Content Provider	Royal Society of Chemistry (RSC)
Author	Wedd, Anthony G. Meulen, Renate van Gottschlich, Lisa Udagedara, Saumya R. Xiao, Zhiguang
Copyright Year	2013
Abstract	Copper plays essential roles in biology, but abnormal interactions are damaging. Reliable quantification of copper–protein interactions will underpin the molecular understanding of copper nutrition and toxicity. We have previously established two high affinity probes, Bathocuproine disulfonate (Bcs) and Bicinchoninate (Bca) anions, that are capable of in vitro quantification of Cu(I) binding with affinities from pico- to atto-molar concentrations. Quantitative probes are required for Cu(I) binding of lower affinity for proteins and peptides typically associated with neurodegenerative diseases. The present work evaluates two classic Fe(II) ligands Ferene S (Fs) and Ferrozine (Fz) as quantitative probes for Cu(I). Both react with Cu(I) quantitatively to yield well-defined complex anions [CuI(Fs)2]3− (λmax = 484 nm, ε = 6700 cm−1 M−1) and [CuI(Fz)2]3− (λmax = 470 nm, ε = 4320 cm−1 M−1). These complexes are sensitive to aerial oxidation (E1/2 ∼ +0.36 V vs. SHE) and to substitution by other ligands (e.g., Cl−, MeCN). However, they can be protected effectively under anaerobic conditions by suitable reductants and an excess of the free probe ligands. Formation constants β2 were determined by two approaches: direct metal ion titration and ligand competition. They provided estimates which differed by ∼3 orders of magnitude. The sources of these differences were examined carefully to consolidate the affinities of the two probes to a unified standard (1015.1 M−2 for Fz and 1013.7 M−2 for Fs). It is apparent that application of direct metal ion titrations to quantification of Cu(I) binding affinities is problematical and should be avoided. The four ligands Bcs, Bca, Fz and Fs in combination form a set of versatile probes for ligand competition experiments and are capable of detecting and differentiating an extended spectrum of Cu(I) binding affinities from nano- to atto-molar concentrations. Selected examples of quantification of weaker Cu(I) binding in proteins and peptides are provided, including that of an amyloid-β peptide.
Starting Page	501
Ending Page	513
Page Count	13
File Format	HTM / HTML PDF
ISSN	17565901
Volume Number	5
Issue Number	5
Journal	Metallomics
DOI	10.1039/c3mt00032j
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Pico- Bca Amyloid beta Anaerobic respiration Ligand Ferrozine Ion Titration Molecular biology Copper Peptide
Content Type	Text
Resource Type	Article
Subject	Chemistry Medicine Metals and Alloys Biochemistry Biomaterials Biophysics

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Evaluation of quantitative probes for weaker Cu(i) binding sites completes a set of four capable of detecting Cu(i) affinities from nanomolar to attomolar

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Evaluation of quantitative probes for weaker Cu(i) binding sites completes a set of four capable of detecting Cu(i) affinities from nanomolar to attomolar