Species-Specific Standard Redox Potential of Thiol-Disulfide Systems: A Key Parameter to Develop Agents against Oxidative Stress

Mirzahosseini, Arash; Noszál, Béla

doi:10.1038/srep37596

Cited by 47 publications

(47 citation statements)

References 21 publications

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“…Physiological solutions contain dissolved O 2 from the air, and thus, Cys‐SH groups of any protein might oxidize spontaneously to form the SS bond(s). The apparent rate constant depends on several microequilibrium constants, which are explicitly not elaborated herein . However, it certainly depends on the width of the conformational space of the reduced molecular fold.…”

Section: Resultsmentioning

confidence: 99%

Compactness of Protein Folds Alters Disulfide‐Bond Reducibility by Three Orders of Magnitude: A Comprehensive Kinetic Case Study on the Reduction of Differently Sized Tryptophan Cage Model Proteins

et al. 2019

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A new approach to monitor disulfide‐bond reduction in the vicinity of aromatic cluster(s) has been derived by using the near‐UV range (λ=266–293 nm) of electronic circular dichroism (ECD) spectra. By combining the results from NMR and ECD spectroscopy, the 3D fold characteristics and associated reduction rate constants (k) of E19_SS, which is a highly thermostable, disulfide‐bond reinforced 39‐amino acid long exenatide mimetic, and its N‐terminally truncated derivatives have been determined under different experimental conditions. Single disulfide bond reduction of the E19_SS model (with an 18‐fold excess of tris(2‐carboxyethyl)phosphine, pH 7, 37 °C) takes hours, which is 20–30 times longer than that expected, and thus, would not reach completion by applying commonly used reduction protocols. It is found that structural, steric, and electrostatic factors influence the reduction rate, resulting in orders of magnitude differences in reduction half‐lives (900>t1/2>1 min) even for structurally similar, well‐folded derivatives of a small model protein.

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Section: Resultsmentioning

confidence: 99%

Compactness of Protein Folds Alters Disulfide‐Bond Reducibility by Three Orders of Magnitude: A Comprehensive Kinetic Case Study on the Reduction of Differently Sized Tryptophan Cage Model Proteins

et al. 2019

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“…For applications in biology, the specific environment of the sensor must be considered. For intracellular environments, the concentrations of GSH are heterogeneous, and the redox values for different molecules change depending on their microscopic environment [ 31 , 56 ]. Instead of examining strong reductants, we selected several salts and amino acids to assess possible issues with selectivity.…”

Section: Resultsmentioning

confidence: 99%

Mn2+-ZnSe/ZnS@SiO2 Nanoparticles for Turn-on Luminescence Thiol Detection

Yazdanparast

Jeffries

Gray

et al. 2017

JFB

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Biological thiols are antioxidants essential for the prevention of disease. For example, low levels of the tripeptide glutathione are associated with heart disease, cancer, and dementia. Mn2+-doped wide bandgap semiconductor nanocrystals exhibit luminescence and magnetic properties that make them attractive for bimodal imaging. We found that these nanocrystals and silica-encapsulated nanoparticle derivatives exhibit enhanced luminescence in the presence of thiols in both organic solvent and aqueous solution. The key to using these nanocrystals as sensors is control over their surfaces. The addition of a ZnS barrier layer or shell produces more stable nanocrystals that are isolated from their surroundings, and luminescence enhancement is only observed with thinner, intermediate shells. Tunability is demonstrated with dodecanethiol and sensitivities decrease with thin, medium, and thick shells. Turn-on nanoprobe luminescence is also generated by several biological thiols, including glutathione, N-acetylcysteine, cysteine, and dithiothreitol. Nanoparticles prepared with different ZnS shell thicknesses demonstrated varying sensitivity to glutathione, which allows for the tuning of particle sensitivity without optimization. The small photoluminescence response to control amino acids and salts indicates selectivity for thiols. Preliminary magnetic measurements highlight the challenge of optimizing sensors for different imaging modalities. In this work, we assess the prospects of using these nanoparticles as luminescent turn-on thiol sensors and for MRI.

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“…It is noted that the direct measurement of the redox potentials for thiol-disulfide systems is not always feasible due to the possible formation of stable metal-thiolate complexes at electrode surfaces [42,43]. Moreover, issues with the direct measurement of redox potentials may exist if the redox reactions being investigated are irreversible or if multiple redox couples are present in solution.…”

Section: Methodsmentioning

confidence: 99%

A Computational Investigation of the Binding of the Selenium Analogues of Ergothioneine and Ovothiol to Cu(I) and Cu(II) and the Effect of Binding on the Redox Potential of the Cu(II)/Cu(I) Redox Couple

Wiebe

Zaliskyy

Bushnell

2019

Journal of Chemistry

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The complexes formed from the binding of ovoselenol (OSeH) and ergoseloneine (ESeH) to Cu(II) and Cu(I) have been investigated with DFT methods. From the calculated thermodynamics, the binding of OSeH and ESeH to Cu(II) and Cu(I) ions increases the reduction potential for the Cu(II)/Cu(I) redox couple. The calculated reduction potentials for the Cu(II)(OSe)2/Cu(I)(OSeH)3+ and Cu(II)(ESe)2/Cu(I)(ESeH)3+ redox couples were found to be 1.15 V and 1.24 V in a dilute aqueous solution. By combining the half reactions for the oxidation of OSeH to the diselenide OSeSeO with the reduction of Cu(II)(OSe)2 to Cu(I)(OSeH)3+, the calculated EMF was 0.90 V. For the oxidation of ESeH to the diselenide ESeSeE with the concomitant reduction of Cu(II)(ESe)2 to Cu(I)(ESeH)3+, the calculated EMF was 0.67 V. Thus, for both systems, the reduction of Cu(II) to Cu(I) with concomitant formation of either diselenide is thermodynamically favourable, and it is expected that both OSeH and ESeH are suitable for the protection against copper induced oxidative damage. As a result, the inhibition of the recycling of Cu(I) to Cu(II) is thermodynamically favourable in the presence of OSeH and ESeH.

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Species-Specific Standard Redox Potential of Thiol-Disulfide Systems: A Key Parameter to Develop Agents against Oxidative Stress

Cited by 47 publications

References 21 publications

Compactness of Protein Folds Alters Disulfide‐Bond Reducibility by Three Orders of Magnitude: A Comprehensive Kinetic Case Study on the Reduction of Differently Sized Tryptophan Cage Model Proteins

Compactness of Protein Folds Alters Disulfide‐Bond Reducibility by Three Orders of Magnitude: A Comprehensive Kinetic Case Study on the Reduction of Differently Sized Tryptophan Cage Model Proteins

Mn2+-ZnSe/ZnS@SiO2 Nanoparticles for Turn-on Luminescence Thiol Detection

A Computational Investigation of the Binding of the Selenium Analogues of Ergothioneine and Ovothiol to Cu(I) and Cu(II) and the Effect of Binding on the Redox Potential of the Cu(II)/Cu(I) Redox Couple

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