Protein-mediated fluorescence resonance energy transfer (P-FRET) probe: fabrication and hydroxyl radical detection
Fluorescent probes based on fluorescence resonance energy transfer (FRET) are highly promising for diverse bioapplications. The key to constructing FRET probes is to confine the donor and acceptor within a sufficiently close distance. However, the commonly used covalent linkage often requires elabor...
Main Authors: | , , , , , , |
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Format: | Journal Article |
Language: | English |
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2023
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Online Access: | https://hdl.handle.net/10356/164113 |
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author | Yu, Xiaokan Zhu, Weisheng Ouyang, Wenao Zhang, Xiaojia Qiu, Hao Zhang, Zhijun Xing, Bengang |
author2 | School of Physical and Mathematical Sciences |
author_facet | School of Physical and Mathematical Sciences Yu, Xiaokan Zhu, Weisheng Ouyang, Wenao Zhang, Xiaojia Qiu, Hao Zhang, Zhijun Xing, Bengang |
author_sort | Yu, Xiaokan |
collection | NTU |
description | Fluorescent probes based on fluorescence resonance energy transfer (FRET) are highly promising for diverse bioapplications. The key to constructing FRET probes is to confine the donor and acceptor within a sufficiently close distance. However, the commonly used covalent linkage often requires elaborate design and complex organic synthesis, and sometimes causes changes in the fluorescence properties of the donor and acceptor. Inspired by the binding between small molecules and protein in nature, herein, we propose a protein-mediated strategy to fabricate FRET probe. In such protein-mediated FRET (P-FRET) probe, protein acts as a carrier to simultaneously confine donor and acceptor in its cavity. As a proof of concept, we use bovine serum albumin (BSA) as a model protein, coumarin derivative as a donor and hydroxyl radical (·OH)-responsive dye fluorescein as an acceptor. Through a series of investigations, including binding parameters, fluorescence properties and detection performance, we prove that the construction of P-FRET probe is simple and feasible and the detection is sensitive. Our P-FRET strategy will provide new insights for the design of FRET probes. |
first_indexed | 2024-10-01T03:45:11Z |
format | Journal Article |
id | ntu-10356/164113 |
institution | Nanyang Technological University |
language | English |
last_indexed | 2024-10-01T03:45:11Z |
publishDate | 2023 |
record_format | dspace |
spelling | ntu-10356/1641132023-01-05T02:38:56Z Protein-mediated fluorescence resonance energy transfer (P-FRET) probe: fabrication and hydroxyl radical detection Yu, Xiaokan Zhu, Weisheng Ouyang, Wenao Zhang, Xiaojia Qiu, Hao Zhang, Zhijun Xing, Bengang School of Physical and Mathematical Sciences School of Chemical and Biomedical Engineering Science::Chemistry Bovine Serum-Albumin Ratiometric Detection Fluorescent probes based on fluorescence resonance energy transfer (FRET) are highly promising for diverse bioapplications. The key to constructing FRET probes is to confine the donor and acceptor within a sufficiently close distance. However, the commonly used covalent linkage often requires elaborate design and complex organic synthesis, and sometimes causes changes in the fluorescence properties of the donor and acceptor. Inspired by the binding between small molecules and protein in nature, herein, we propose a protein-mediated strategy to fabricate FRET probe. In such protein-mediated FRET (P-FRET) probe, protein acts as a carrier to simultaneously confine donor and acceptor in its cavity. As a proof of concept, we use bovine serum albumin (BSA) as a model protein, coumarin derivative as a donor and hydroxyl radical (·OH)-responsive dye fluorescein as an acceptor. Through a series of investigations, including binding parameters, fluorescence properties and detection performance, we prove that the construction of P-FRET probe is simple and feasible and the detection is sensitive. Our P-FRET strategy will provide new insights for the design of FRET probes. Agency for Science, Technology and Research (A*STAR) Ministry of Education (MOE) Z.Z. acknowledges the financial support from National Natural Science Foundation of China (NSFC) (No. 22007083), Zhejiang Provincial Natural Science Foundation of China (Grant No. LQ20B010010) and Science Foundation of Zhejiang Sci-Tech University (ZSTU) under Grant No. 19062410-Y. B.X. acknowledges the financial support from Tier 1, RG6/20, A*Star SERC A1983c0028 (M4070319), A20E5c0090, National Natural Science Foundation of China (NSFC) (No. 51929201). 2023-01-05T02:38:56Z 2023-01-05T02:38:56Z 2022 Journal Article Yu, X., Zhu, W., Ouyang, W., Zhang, X., Qiu, H., Zhang, Z. & Xing, B. (2022). Protein-mediated fluorescence resonance energy transfer (P-FRET) probe: fabrication and hydroxyl radical detection. Photochemistry and Photobiology, 98(2), 371-377. https://dx.doi.org/10.1111/php.13595 0031-8655 https://hdl.handle.net/10356/164113 10.1111/php.13595 35064566 2-s2.0-85123930755 2 98 371 377 en RG6/20 A1983c0028 (M4070319) A20E5c0090 Photochemistry and Photobiology © 2022 American Society for Photobiology. All rights reserved. |
spellingShingle | Science::Chemistry Bovine Serum-Albumin Ratiometric Detection Yu, Xiaokan Zhu, Weisheng Ouyang, Wenao Zhang, Xiaojia Qiu, Hao Zhang, Zhijun Xing, Bengang Protein-mediated fluorescence resonance energy transfer (P-FRET) probe: fabrication and hydroxyl radical detection |
title | Protein-mediated fluorescence resonance energy transfer (P-FRET) probe: fabrication and hydroxyl radical detection |
title_full | Protein-mediated fluorescence resonance energy transfer (P-FRET) probe: fabrication and hydroxyl radical detection |
title_fullStr | Protein-mediated fluorescence resonance energy transfer (P-FRET) probe: fabrication and hydroxyl radical detection |
title_full_unstemmed | Protein-mediated fluorescence resonance energy transfer (P-FRET) probe: fabrication and hydroxyl radical detection |
title_short | Protein-mediated fluorescence resonance energy transfer (P-FRET) probe: fabrication and hydroxyl radical detection |
title_sort | protein mediated fluorescence resonance energy transfer p fret probe fabrication and hydroxyl radical detection |
topic | Science::Chemistry Bovine Serum-Albumin Ratiometric Detection |
url | https://hdl.handle.net/10356/164113 |
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