Chronopotentiometric sensing of native, oligomeric, denatured and aggregated serum albumin at charged surfaces
Language English Country Netherlands Media print-electronic
Document type Journal Article
PubMed
35334293
DOI
10.1016/j.bioelechem.2022.108100
PII: S1567-5394(22)00051-2
Knihovny.cz E-resources
- Keywords
- Charged surface, Constant current chronopotentiometry, Electrode, Freezing, Scanning transmission electron microscopy, Serum albumin,
- MeSH
- Adsorption MeSH
- Protein Denaturation MeSH
- Peptides MeSH
- Serum Albumin, Bovine * chemistry MeSH
- Serum Albumin * MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Peptides MeSH
- Serum Albumin, Bovine * MeSH
- Serum Albumin * MeSH
In protein analysis, fast techniques applicable for preliminary tests of the protein structural changes are sought. We show that using constant current chronopotentiometric stripping peak H, small amounts of oligomeric, denatured and aggregated bovine serum albumin (BSA) can be easily distinguished from native form. Different behavior of native, denatured, and aggregated BSA could be explained by combination of their different adsorption at charged surface and accessibility of electroactive amino acid residues. Ability to discriminate between individual forms allows to use chronopotentiometric stripping for study of processes responsible for structural changes, such as freezing treatment.
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