Electrocatalytic assay for monitoring methylglyoxal-mediated protein glycation
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
25539570
DOI
10.1021/ac503705d
Knihovny.cz E-zdroje
- MeSH
- biotest * MeSH
- elektrochemie MeSH
- elektrody * MeSH
- glykosylace účinky léků MeSH
- glykovaný sérový albumin MeSH
- guanidiny farmakologie MeSH
- inhibitory enzymů farmakologie MeSH
- katalýza MeSH
- konformace proteinů MeSH
- lidé MeSH
- molekulární modely MeSH
- molekulární sekvence - údaje MeSH
- muramidasa analýza chemie MeSH
- produkty pokročilé glykace MeSH
- pyruvaldehyd farmakologie MeSH
- sekvence aminokyselin MeSH
- sérový albumin hovězí analýza chemie MeSH
- sérový albumin analýza chemie MeSH
- skot MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- skot MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- glykovaný sérový albumin MeSH
- guanidiny MeSH
- inhibitory enzymů MeSH
- muramidasa MeSH
- pimagedine MeSH Prohlížeč
- produkty pokročilé glykace MeSH
- pyruvaldehyd MeSH
- sérový albumin hovězí MeSH
- sérový albumin MeSH
Protein glycation is a complex process that plays an important role in diabetes mellitus, aging, and the regulation of protein function in general. As a result, current methodological research on proteins is focused on the development of novel approaches for investigating glycation and the possibility of monitoring its modulation and selective inhibition. In this paper, a first sensing strategy for protein glycation is proposed, based on protein electroactivity measurement. Concretely, the label-free method proposed is based on the application of a constant-current chronopotentiometric stripping (CPS) analysis at Hg-containing electrodes. The glycation process was monitored as the decrease in the electrocatalytic protein signal, peak H, observed at highly negative potentials at around -1.8 V (vs Ag/AgCl3 M KCl), which was previously ascribed to a catalytic hydrogen evolution reaction (CHER). Using this method, a model protein bovine serum albumin was investigated over 3 days of incubation with the glycation agent methylglyoxal in the absence or presence of the glycation inhibitor aminoguanidine (pimagedine). The electrochemical methodology presented here could open up new possibilities in research on protein glycation and oxidative modification. The methodology developed also provides a new option for the analysis of protein intermolecular interactions using electrochemical sensors, which was demonstrated by the application of a silver solid amalgam electrode (AgSAE) for monitoring the glycation process in samples of bovine serum albumin, human serum albumin, and lysozyme.
Citace poskytuje Crossref.org
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