Silicon Nanowire Field-Effect Transistor as Biosensing Platforms for Post-Translational Modification

Ping Chia Su, Bo Han Chen, Yi Chan Lee, Yuh Shyong Yang

Research output: Contribution to journalArticlepeer-review

8 Scopus citations


Protein tyrosine sulfation (PTS), a vital post-translational modification, facilitates protein-protein interactions and regulates many physiological and pathological responses. Monitoring PTS has been difficult owing to the instability of sulfated proteins and the lack of a suitable method for detecting the protein sulfate ester. In this study, we combined an in situ PTS system with a high-sensitivity polysilicon nanowire field-effect transistor (pSNWFET)-based sensor to directly monitor PTS formation. A peptide containing the tyrosine sulfation site of P-selectin glycoprotein ligand (PSGL)-1 was immobilized onto the surface of the pSNWFET by using 3-aminopropyltriethoxysilane and glutaraldehyde as linker molecules. A coupled enzyme sulfation system consisting of tyrosylprotein sulfotransferase and phenol sulfotransferase was used to catalyze PTS of the immobilized PSGL-1 peptide. Enzyme-catalyzed sulfation of the immobilized peptide was readily observed through the shift of the drain current-gate voltage curves of the pSNWFET before and after PTS. We expect that this approach can be developed as a next generation biochip for biomedical research and industries.

Original languageEnglish
Issue number12
StatePublished - 21 Dec 2020


  • polycrystalline silicon nanowire field-effect transistor (pSNWFET)
  • post-translational modifications (PTMs)
  • protein tyrosine sulfation (PTS)
  • protein–protein interaction


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