Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

Silicon Nanowire Field-Effect Transistor as Next Generation Biochip for Post-Translational Modification

Version 1 : Received: 3 November 2020 / Approved: 3 November 2020 / Online: 3 November 2020 (14:36:25 CET)

How to cite: Su, P.; Chen, B.; Lee, Y.; Yang, Y. Silicon Nanowire Field-Effect Transistor as Next Generation Biochip for Post-Translational Modification. Preprints 2020, 2020110162 (doi: 10.20944/preprints202011.0162.v1). Su, P.; Chen, B.; Lee, Y.; Yang, Y. Silicon Nanowire Field-Effect Transistor as Next Generation Biochip for Post-Translational Modification. Preprints 2020, 2020110162 (doi: 10.20944/preprints202011.0162.v1).

Abstract

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 an ultra-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. To the best of our knowledge, this is the first study to describe in situ PTS and its direct observation by using semiconductor devices. We expect that this approach can be developed as a next generation biochip for biomedical research and industries.

Subject Areas

Posttranslational modifications (PTMs); Protein tyrosine sulfation (PTS); Protein–protein interaction

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