Complexation Properties of the Metallothionein Fragment Lys-Cys-Thr-Cys-Cys-Ala [56-61] MT I with Zinc and Cadmium Using Square Wave Voltammetry

Nieto, Óscar; Rodríguez, A. R.

doi:10.1002/(sici)1521-4109(199903)11:3<175::aid-elan175>3.0.co;2-k

Cited by 13 publications

(9 citation statements)

References 19 publications

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“…3A f), the peak potential does not coincide with the one of free Zn 2+ but shifts to more positive values than are attributed to Znβ'. This behaviour was already noticed during zinc and cadmium additions to MT or FT; nevertheless the peak labelled Zn is not clearly associated with Zn 2+ nor with a weak complex of zinc with the organic molecules [12,15,20,24].…”

Section: Resultsmentioning

confidence: 73%

“…In this figure, the new peak labelled Cdβ' is shown and is attributed to the reduction of cadmium complexed by the β domain in a different complexation form to the Cdβ one. This new peak is labelled Cdβ' by analogy with peaks named CdT and CdT' in the study of MT [8][9][10][11][12][13][14][15][16] and CdFT and CdFT' obtained with the peptidic fragment FT in the presence of cadmium and/or zinc [17][18][19][20][21][22][23][24][25] in previous electrochemical works. Peaks have been resolved as mentioned and it is necessary to point out that, when Zn 2+ is in excess (Fig.…”

Section: Resultsmentioning

confidence: 88%

“…When the β domain is solely present in the supporting electrolyte, the peak named β is only observed in some cases using DPP; however if square wave voltammetry is used, this β peak is very well defined and detected at -709 mV (results not shown). This peak is attributed to the oxidation of the mercury electrode in the presence of free thiol groups and due to an adsorption process [14,[20][21][22][23][24].…”

Section: Resultsmentioning

confidence: 99%

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Complexing properties of the b metallothionein domain with cadmium and/or zinc, studied by differential pulse polarography

Dabrio¹,

Rodríguez²

2000

Analusis

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Mammalian metallothioneins (MT) containing 61 amino acids, of which 20 are cysteine have a structure comprising of two clusters. The α clusters correspond to the C terminal domain of residues 31-61 involving eleven cysteinic residues and the β cluster corresponds to the N-terminal domain of residues 1-30 with nine cysteine residues. All twenty cysteines participate in metal binding. While in the case of MT, their structure and characteristics have been studied using a great variety of analytical methods [1][2][3][4][5][6][7], relatively few studies have been performed with the α and β clusters separately probably due to the difficulties associated with their obtention. In fact these two domains are usually obtained by synthesis using either solid-phase and fragmentcondensation techniques or isolated by proteolysis of metallothioneins of different origin. Nevertheless the use of chemically synthesised and well-characterised separate α and β domains could be very interesting for the study of their metal binding properties and therefore contribute to the understanding of the behaviour of the entire MT.The aim of this research is the systematic study of the complexing properties of the β MT domain with cadmium and/or zinc using electroanalytical methods. These methods have been widely used by our team for the investigation of MT [8][9][10][11][12][13][14][15][16] and related molecules such as the peptidic fragment Lys-Cys-Thr-Cys-Ala (56-61) MT-1 (FT) alone and in the presence of cadmium and/or zinc [17][18][19][20][21][22][23][24][25]. In the case of MT and related molecules, the aminoacid chain is electroactive due to the presence of thiol groups. Moreover, the reduction of the cations, cadmium and zinc, is electrochemically reversible at the mercury electrode and, hence it is possible to obtain three different responses simultaneously for the sample under a given set of experimental conditions. In addition, the electrochemical response depends on the chemical form of the element and allows one to monitor the changes of the different species in solution as a function of different parameters.The β domain has been isolated using different methods [3,7] and its binding properties have been investigated using mainly spectroscopic methods [3,7,[26][27][28][29][30][31][32][33]. The synthesised peptide used in this work has been purchased from the Biochemistry Institute of Zurich University. The purity of this molecule was checked by both Dr. Klauser's team from Zurich University and our team using electrospray ionisation mass spectrometry (ESI-MS) [34,35].The binding properties have been studied, using differential pulse polarography, with different types of additions of metal ions to the apo-β domain and the inverted addition of the β MT domain to metal ions, the gradual addition of metal ions separately and the addition of both cations simultaneously.

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Section: Resultsmentioning

confidence: 73%

Section: Resultsmentioning

confidence: 88%

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Complexing properties of the b metallothionein domain with cadmium and/or zinc, studied by differential pulse polarography

Dabrio¹,

Rodríguez²

2000

Analusis

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“…Previous electrochemical studies that have investigated the solution complexation properties of metallothionein derived peptides have also reported shifts in the peak potential with variation in the heavy metal ion concentration. [38,39] To assess the durability of the peptide-functionalized polymer brush coatings, cyclic voltammograms were recorded over up to 10 cycles by exposing a coated AuNP-IrMA to an 8 mM Hg 2þ solution. As indicated in Fig.…”

Section: Cyclic Voltammetry (Cv)mentioning

confidence: 99%

Voltammetric Detection of Hg2+ Using Peptide-Functionalized Polymer Brushes

Schüwer¹,

Tercier‐Waeber²,

Danial³

et al. 2012

Aust. J. Chem.

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Polymer brushes grafted by surface-initiated atom transfer radical polymerization (SI-ATRP) from the surface of Ir-based microelectrode arrays are explored as a platform for the fabrication of sensory coatings for the voltammetric detection of Hg 2þ . The polymer brush coatings are post-modified with a metallothionein derived peptide to enable the selective detection of Hg 2þ . The performance of the polymer brush modified microelectrode arrays was evaluated using both cyclic voltammetry (CV) as well as square-wave anodic stripping voltammetry (SWASV) experiments. These studies revealed that the polymer brush based coatings allowed the selective detection of Hg 2þ with detection limits in the subnanomolar range.

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“…Differential pulse polarography (DPP) is the most extensively used in the characterization of Cd,ZnMT, CdMT and ZnMT from diverse origins [1 ± 6] as well as in Cd-FT, Zn-FT and Cd,ZnFT [7 ± 11] or Cd-GSH and Zn-GSH [12 ± 15]. Other techniques such as square-wave voltammetry (SWV) [16,17] or cyclic voltammetry (CV) [18 ± 21] have also been applied. In addition to the above mentioned techniques, cathodic (CSV) and anodic (ASV) stripping voltammetry have also been used to characterize the Cd-, Pb-, Zn-and Cu-Phytochelatines metal complexation equilibria [22 ± 24].…”

Section: Introductionmentioning

confidence: 99%

Comparison of Voltammetry Assisted by Multivariate Analysis with EXAFS as Applied to the Study of Cd- and Zn-Binding of Metallothionein Related Peptides

2002

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Complexation Properties of the Metallothionein Fragment Lys-Cys-Thr-Cys-Cys-Ala [56-61] MT I with Zinc and Cadmium Using Square Wave Voltammetry

Cited by 13 publications

References 19 publications

Complexing properties of the b metallothionein domain with cadmium and/or zinc, studied by differential pulse polarography

Complexing properties of the b metallothionein domain with cadmium and/or zinc, studied by differential pulse polarography

Voltammetric Detection of Hg2+ Using Peptide-Functionalized Polymer Brushes

Comparison of Voltammetry Assisted by Multivariate Analysis with EXAFS as Applied to the Study of Cd- and Zn-Binding of Metallothionein Related Peptides

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