Silicon Nanowire Field-Effect Transistor as Biosensing Platforms for Post-Translational Modification
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 detec...
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| Format: | Article |
| Language: | English |
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MDPI AG
2020-12-01
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| Series: | Biosensors |
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| Online Access: | https://www.mdpi.com/2079-6374/10/12/213 |
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| author | Ping-Chia Su Bo-Han Chen Yi-Chan Lee Yuh-Shyong Yang |
| author_facet | Ping-Chia Su Bo-Han Chen Yi-Chan Lee Yuh-Shyong Yang |
| author_sort | Ping-Chia Su |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-10T13:53:46Z |
| format | Article |
| id | doaj.art-d7c59d9dc0e14c1b8c60569a80ff650b |
| institution | Directory Open Access Journal |
| issn | 2079-6374 |
| language | English |
| last_indexed | 2024-03-10T13:53:46Z |
| publishDate | 2020-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biosensors |
| spelling | doaj.art-d7c59d9dc0e14c1b8c60569a80ff650b2023-11-21T01:52:34ZengMDPI AGBiosensors2079-63742020-12-01101221310.3390/bios10120213Silicon Nanowire Field-Effect Transistor as Biosensing Platforms for Post-Translational ModificationPing-Chia Su0Bo-Han Chen1Yi-Chan Lee2Yuh-Shyong Yang3Department of Biological Science and Technology, National Chiao Tung University, Hsinchu 300, TaiwanDepartment of Biological Science and Technology, National Chiao Tung University, Hsinchu 300, TaiwanDepartment of Biological Science and Technology, National Chiao Tung University, Hsinchu 300, TaiwanDepartment of Biological Science and Technology, National Chiao Tung University, Hsinchu 300, TaiwanProtein 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.https://www.mdpi.com/2079-6374/10/12/213polycrystalline silicon nanowire field-effect transistor (pSNWFET)post-translational modifications (PTMs)protein tyrosine sulfation (PTS)protein–protein interaction |
| spellingShingle | Ping-Chia Su Bo-Han Chen Yi-Chan Lee Yuh-Shyong Yang Silicon Nanowire Field-Effect Transistor as Biosensing Platforms for Post-Translational Modification Biosensors polycrystalline silicon nanowire field-effect transistor (pSNWFET) post-translational modifications (PTMs) protein tyrosine sulfation (PTS) protein–protein interaction |
| title | Silicon Nanowire Field-Effect Transistor as Biosensing Platforms for Post-Translational Modification |
| title_full | Silicon Nanowire Field-Effect Transistor as Biosensing Platforms for Post-Translational Modification |
| title_fullStr | Silicon Nanowire Field-Effect Transistor as Biosensing Platforms for Post-Translational Modification |
| title_full_unstemmed | Silicon Nanowire Field-Effect Transistor as Biosensing Platforms for Post-Translational Modification |
| title_short | Silicon Nanowire Field-Effect Transistor as Biosensing Platforms for Post-Translational Modification |
| title_sort | silicon nanowire field effect transistor as biosensing platforms for post translational modification |
| topic | polycrystalline silicon nanowire field-effect transistor (pSNWFET) post-translational modifications (PTMs) protein tyrosine sulfation (PTS) protein–protein interaction |
| url | https://www.mdpi.com/2079-6374/10/12/213 |
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