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

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

doi:10.3390/bios10120213

Ping-Chia Su, Yi-Chan Lee + Show 2 more

Open Access

https://doi.org/10.3390/bios10120213

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Journal: Biosensors	Publication Date: Dec 21, 2020
Citations: 11	License type: CC BY 4.0

Affiliation: National Yang Ming Chiao Tung University

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 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.

Highlights

Protein tyrosine sulfation (PTS), a common post-translational modification (PTM), regulates numerous physiological responses and pathological diseases [1,2,3]
PTS participates in some protein–protein interactions including hemostasis, leukocyte rolling on endothelial cells, ligand binding to receptors, visual functions, inflammatory responses, and viral entry into host cells [1,2,5,6,7,8,9]
Through the use of atomic force microscopy (AFM), it was discovered that tyrosylprotein sulfotransferase (TPST)-induced protein–protein interactions were mainly caused by the sulfation of Y-51 within P-selectin glycoprotein ligand (PSGL)-1 [28,29]. These results suggested that PSGL-1 is a PTS substrate, and self-assembled monolayers (SAMs) can be applied to immobilize proteins onto the silicon surface; PTS reactions can be conducted on the silicon surface

Summary

Introduction

Protein tyrosine sulfation (PTS), a common post-translational modification (PTM), regulates numerous physiological responses and pathological diseases [1,2,3]. The occurrence of PTS was estimated to be up to 1% of total tyrosine and approximately 30% of proteins [3]. PTS participates in some protein–protein interactions including hemostasis, leukocyte rolling on endothelial cells, ligand binding to receptors, visual functions, inflammatory responses, and viral entry into host cells [1,2,5,6,7,8,9]. PTS was reported to facilitate infection with the human immunodeficiency virus (HIV) and enterovirus (EV) 71 [2]. PTS of C–C chemokine receptor type 5 (CCR5) is involved in the entry of HIV-1 into CD4+ cells.

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