Electrocatalytic assay for monitoring methylglyoxal-mediated protein glycation
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
25539570
DOI
10.1021/ac503705d
Knihovny.cz E-resources
- MeSH
- Biological Assay * MeSH
- Electrochemistry MeSH
- Electrodes * MeSH
- Glycosylation drug effects MeSH
- Glycated Serum Albumin MeSH
- Guanidines pharmacology MeSH
- Enzyme Inhibitors pharmacology MeSH
- Catalysis MeSH
- Protein Conformation MeSH
- Humans MeSH
- Models, Molecular MeSH
- Molecular Sequence Data MeSH
- Muramidase analysis chemistry MeSH
- Glycation End Products, Advanced MeSH
- Pyruvaldehyde pharmacology MeSH
- Amino Acid Sequence MeSH
- Serum Albumin, Bovine analysis chemistry MeSH
- Serum Albumin analysis chemistry MeSH
- Cattle MeSH
- Animals MeSH
- Check Tag
- Humans MeSH
- Cattle MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Glycated Serum Albumin MeSH
- Guanidines MeSH
- Enzyme Inhibitors MeSH
- Muramidase MeSH
- pimagedine MeSH Browser
- Glycation End Products, Advanced MeSH
- Pyruvaldehyde MeSH
- Serum Albumin, Bovine MeSH
- Serum 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.
References provided by Crossref.org
Redox properties and human serum albumin binding of nitro-oleic acid
