Electrochemical behaviour of proteins at graphite electrodes. I. Electrooxidation of proteins as a new probe of protein structure and reactions

Brabec, Viktor; Mornstein, Vojtěch

doi:10.1016/0005-2795(80)90106-3

Cited by 93 publications

(59 citation statements)

References 6 publications

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“…In Trp the indole ring was susceptible to electrooxidation from its heteroatom [82,83]. Electrooxidation of Tyr residues involved one electron and single proton transfer (showing similarity to the electrode process responsible for the electrooxidation of simple p-substituted phenols) [84].…”

Section: Electrooxidation Of Peptides and Proteins At Solid Electrodesmentioning

confidence: 90%

“…Electrooxidation of Tyr residues involved one electron and single proton transfer (showing similarity to the electrode process responsible for the electrooxidation of simple p-substituted phenols) [84]. It was found that among the amino acids (aa) usually occurring in proteins, in addition to Tyr and Trp, histidine, cysteine and methionine yielded voltammetric oxidation peaks in their free states but not when incorporated in proteins [82]. Other free aas did not yield any peak in the range of pH 4 -10.…”

Section: Electrooxidation Of Peptides and Proteins At Solid Electrodesmentioning

confidence: 95%

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Electroactivity of Nonconjugated Proteins and Peptides. Towards Electroanalysis of All Proteins

2007

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Present proteomics and biomedicine require sensitive analytical methods for all proteins. Recent progress in electrochemical analysis of peptides and proteins based on their intrinsic electroactivity is reviewed. Tyrosine and/or tryptophan-containing proteins are oxidizable at carbon electrodes. At mercury electrodes all peptides and proteins (about 13 peptides and > 25 proteins were tested) produce chronopotentiometric peak H at nanomolar concentrations. This peak is sensitive to changes in protein structure. Microliter sample volumes are sufficient for the analysis. Electrochemical methods can be used in studies of nucleic acid-protein interactions and can be applied in biomedicine. Examples of such applications in neurogenerative diseases and cancer are presented.

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Section: Electrooxidation Of Peptides and Proteins At Solid Electrodesmentioning

confidence: 90%

Section: Electrooxidation Of Peptides and Proteins At Solid Electrodesmentioning

confidence: 95%

Electroactivity of Nonconjugated Proteins and Peptides. Towards Electroanalysis of All Proteins

2007

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“…In 1980 it was shown that tyrosine and tryptophan residues in proteins could be oxidized at carbon electrodes [12,13]. Voltammetric methods have been, however, not capable of producing well-resolved peaks of tyrosine and tryptophan and to determine peptides and proteins at submicromolar concentrations.…”

Section: Introductionmentioning

confidence: 99%

Constant Current Chronopotentiometric Stripping Analysis of Bioactive Peptides at Mercury and Carbon Electrodes

et al. 1998

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Constant current derivative chronopotentiometric stripping analysis (CPSA) was used to study bioactive peptides [Lys 8 ]-vasopressin and angiotensin II at carbon paste electrode (CPE) and hanging mercury drop electrode (HMDE). Both peptides contain a single tyrosine residue which is oxidized at CPE close to þ0.6 V (against Ag/AgCl/3 M KCl electrode) producing peak Y; this peak was by about 15 mV more positive in vasopressin than in angiotensin II. At HMDE vasopressin yielded peak S due to the reduction of the disulfidic bond in the peptide. No peak S was observed with angiotensin II as it does not contain any cystine/cysteine residues. Vasopressin produced different catalytic hydrogen reduction signals in media with cobalt ion and in media not containing any metal ion. The signal produced in the latter media (peak H), which appeared close to ¹1.7 V, was well separated from the background. No catalytic hydrogen reduction signal was obtained with angiotensin II. The above mentioned CPSA signals can be applied for the determination of the respective peptide at nanomolar concentrations. The least sensitive peak S appears which requires at least 100 nM vasopressin concentration at moderate accumulation time. By two orders of magnitude, higher sensitivities can be obtained with peaks Y and H. In measuring these peaks CPSA shows significant advantages over the voltammetric stripping techniques.

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“…Both of these amino acids can be detected by amperometry with carbon electrodes at potentials 5 1.0 V [5]. Peptides containing tryptophan and/or tyrosine in positions that are accessible to an electrode surface can therefore be detected based on oxidation of these electroactive side chains [2]. Since many neuropeptides and hormones, including enkephalins, endorphins, melanocyte stimulating hormone (MSH), and cholecystokinin, are small peptides that contain tyrosine or tryptophan, improved electrochemical methods could be of benefit in the study of these important compounds.…”

Section: Introductionmentioning

confidence: 99%

Amperometry and cyclic voltammetry of tyrosine and tryptophan‐containing oligopeptides at carbon fiber microelectrodes applied to single cell analysis

Paras

Kennedy

1997

Electroanalysis

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The amperometric and cyclic voltammetric detection of a-melanocyte stimulating hormone (MSH), 0-endorphin, and corticotropin-like intermediate lobe peptide (CLIP), all proopiocortin (POC) derived peptides secreted from melanocytes of the pituitary intermediate lobe, at carbon fiber microelectrodes was investigated. For amperometry, it was found that all of these peptides could be detected; however, fouling of the electrodes reduced the response of the electrode after successive application of the peptide in flow injection experiments. The fouling wa5 apparently due to oxidation of tyrosine in the peptides as similar results were found for tyrosine but not tryptophan. The effect of fouling could be reversed if the electrode was electrochemically treated by scanning from -1 .OV to +1.OV at 300 V/s for 2 min between application of the peptides. Using cyclic voltammtery at 800 V/s, it was possible to distinguish MSH, which had a peak shaped voltammogram, from the other POC peptides, which had relatively flat voltammetric waves at this scan rate. The scan rate dependence of the peak current for MSH revealed that the voltammetry was adsorption controlled. As a result, in a monitoring application, where voltammograms are continuously obtained with a fixed interval between them, decreasing the interval increases the temporal resolution but decreases the sensitivity for MSH. It was found that when monitoring the current in the potential range of 0.90 to 1 .OOV, the temporal response to MSH was dependent upon the potential window used for scanning. Using high scan rates and a potential window of 0 to 1.2 V, it was possible to monitor exocytosis from single melanocytes and use the voltammogram to demonstrate detection of MSH from the cells.

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Electrochemical behaviour of proteins at graphite electrodes. I. Electrooxidation of proteins as a new probe of protein structure and reactions

Cited by 93 publications

References 6 publications

Electroactivity of Nonconjugated Proteins and Peptides. Towards Electroanalysis of All Proteins

Electroactivity of Nonconjugated Proteins and Peptides. Towards Electroanalysis of All Proteins

Constant Current Chronopotentiometric Stripping Analysis of Bioactive Peptides at Mercury and Carbon Electrodes

Amperometry and cyclic voltammetry of tyrosine and tryptophan‐containing oligopeptides at carbon fiber microelectrodes applied to single cell analysis

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