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- W3206972882 abstract "• Glycoproteins, fetuin and asialofetuin, were studied at charged surfaces. • Their chronopotentiometric responses, peaks H, and impedance C - t curves differed. • Behavior of these proteins was affected by sialic acid presence in their glycan part. • Fetuin showed higher stability against electric field effects than sialofetuin. Major human diseases are associated with changes in glycosylation. The sialic acid is highly expressed saccharide residue typically terminating branches of protein glycans and glycosphingolipids. Here we compared sialoprotein fetuin with its desialylated form – asialofetuin using label-free constant current chronopotentiometric stripping (CPS) analysis and impedance C - t curves to better understand the behavior of glycoproteins at charged surfaces. Electrochemistry represents useful tool for study of molecules at charged surfaces. Using CPS peak H, we show that the terminal sialic acids presence in glycans of fetuin stabilizes its molecule against effects of electric field. Additionally the presence of negatively charged sialic acid prevents an interaction between glycoprotein and negatively charged electrode. The different behavior of the glycoproteins according to sialic acid content can also be used for easy determination of sialoglycoproteins." @default.
- W3206972882 created "2021-10-25" @default.
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- W3206972882 date "2021-12-01" @default.
- W3206972882 modified "2023-10-17" @default.
- W3206972882 title "Fetuin and asialofetuin at charged surfaces: Influence of sialic acid presence" @default.
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- W3206972882 doi "https://doi.org/10.1016/j.jelechem.2021.115801" @default.
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