겨울 심포지움
2018겨울초록
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포스터발표 |
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공동저자
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접수자
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Phosphorylation is one of the most important post-translational modifications(PTMs) of proteins, which modulates a wide range of biological functions and activity of proteins. The analysis of phosphopeptides is still one of the most challenging tasks in proteomics research by mass spectrometry. In this study, phosphopeptide enrichment approach on a digital microfluidic(DMF) chip was demonstrated by analyzing phosphopeptides in the tryptic digested β-casein(bovine) and Ovalbumin(chicken). This approach was made using a magnetic beads(MB)-based titanium dioxide(TiO2)-solid phase extraction(SPE) procedure. TiO2-MB was employed to selectively isolate phosphopeptides from tryptic digests of β-casein and Ovalbumin. Droplet operation on a chip was made by the technique of mixing the magnetic bead and the liquid droplet, the technique of collecting the magnetic beads using a neodium magnet, and the technique of separating the magnetic beads and droplet. The enriched phosphopeptides were detected using matrix-assisted laser desorption ionization time-of-flight mass spectrometry(MALDI-TOF MS). This study shows that the phosphopeptide enrichment analysis can be automated and analyzed with a small sample volume.
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