Electrochemical modifications of proteins: disulfide bonds reduction

Cayot, Philippe; Rosier, Hélène; Roullier, L.; Haertlé, Thomas; Tainturier, G.

doi:10.1016/s0308-8146(01)00352-1

Cited by 18 publications

(13 citation statements)

References 36 publications

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“…A similar procedure was reported previously. 23, 24 On the basis of the ESMS results, the pathway of S-S bond cleavage in GSSG is described in Scheme 1. The HPLC chromatogram of the reaction between [Pt-(Met)Cl 2 ] and GSSG showed that at least four species appeared within 24 h, but the peaks are barely identifiable except that of GSSG (retention time of 1.35 min).…”

Section: Discussionmentioning

confidence: 99%

Disulfide Bond Cleavage Induced by a Platinum(II) Methionine Complex

et al. 2005

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The cleavage of a disulfide bond and the redox equilibrium of thiol/disulfide are strongly related to the levels of glutathione (GSH)/oxidized glutathione (GSSG) or mixed disulfides in vivo. In this work, the cleavage of a disulfide bond in GSSG induced by a platinum(II) complex [Pt(Met)Cl2] (where Met = methionine) was studied and the cleavage fragments or their platinated adducts were identified by means of electrospray mass spectrometry, high-performance liquid chromatography, and ultraviolet techniques. The second-order rate constant for the reaction between [Pt(Met)Cl2] and GSSG was determined to be 0.4 M(-1) s(-1) at 310 K and pH 7.4, which is 100- and 12-fold faster than those of cisplatin and its monoaqua species, respectively. Different complexes were formed in the reaction of [Pt(Met)Cl2] with GSSG, mainly mono- and dinuclear platinum complexes with the cleavage fragments of GSSG. This study demonstrated that [Pt(Met)Cl2] can promote the cleavage of disulfide bonds. The mechanistic insight obtained from this study may provide a deeper understanding on the potential involvement of platinum complexes in the intracellular GSH/GSSG systems.

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Section: Discussionmentioning

confidence: 99%

Disulfide Bond Cleavage Induced by a Platinum(II) Methionine Complex

et al. 2005

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“…Thus, it seems that the effect of increasing voltage during the superimposition of an electrical field upon cross-flow membrane filtration of a complex peptide mixture results not only in a higher fractionation due to the higher electrical field applied but also in a higher chemical modification of the peptides. This leads to a lower concentration of the original peptides, which is in accordance to Cayot et al (1999Cayot et al ( , 2002 and Hawkins et al (2003).…”

Section: Determination Of Lactose Modification Via Hplcmentioning

confidence: 54%

“…As a result, molecular water splitting is processing faster due to the ions, which again carry electrical voltage. In the case of solutions containing proteins, peptides, or amino acids, this effect may also influence the chemical modification of molecules to be fractionated by an electrical field (Bazinet et al 1997a, b;Cayot et al 1999Cayot et al , 2002. In detail, hypochlorite-induced oxidation of peptides depends on the amino acid sequence of these peptides and their reactive side chains.…”

Section: Introductionmentioning

confidence: 99%

Electrochemical modification of dairy-based functional peptides by means of cross-flow electro membrane filtration

Holder

Großmann

Weiß

et al. 2014

Dairy Sci. & Technol.

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International audienceThe stability of functional peptides against electrochemical modification during their selective fractionation via cross-flow electro membrane filtration is a prerequisite for their successful application in food products to ensure the bio-functionality, emulsification, foam formation, or stabilizing properties. This study investigated the impact of electrical fields applied to cross-flow membrane filtration on electrolysis and the associated electrochemical modification of functional dairy-based peptides to calculate the electrical load of target analytes during the process. Firstly, electrolysis and the hypochlorite-induced oxidation of the model peptide β-CN f(108–113) and lactose at different hypochlorite concentrations were studied under well-controlled laboratory conditions, followed by the electrochemical modification of functional peptides during cross-flow electro membrane filtration. At laboratory conditions, a chemical modification of the model peptide β-CN f(108–113) below a value of 3 mol.L−1 hypochlorite was not observed, while lactose was modified at minimal hypochlorite concentrations and, thus, acted as a protection group for peptides. The electrochemical modification of functional peptides was only observed for voltages ≥10 V in cross-flow electro membrane filtration experiments. In addition, results indicate that a further increase in electrical voltage (>5 V) does not result in a significant improvement of peptide electrophoresis, and thus, there is no higher fractionation of functional peptides. These experiments show that under optimal conditions of filtration with a superimposed electrical field, no chemical modification of functional peptides takes place that indicates an advantage compared to conventional filtration processes by significantly increasing the fractionation efficiency at voltages between 5 and 7 V

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“…We can expect to exploit the protolytic effect of the oxidized thiols due to possibility of cleavage of the disulfide bond -S-Son the MMCFE surface with its subsequent eventual protonation [38]. The oxidised thiols studies, HCySS and GSSG, have more accentuated differences in comparison with the similarities registered for the reduced thiols.…”

Section: Cyclic Voltammetry Of Oxidized Thiolsmentioning

confidence: 99%