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We developed the fluorogenic SNAP probe BGAN-8C to monitor protein degradation. It exhibited a 6-fold fluorescence enhancement upon binding with SNAP-tag. After the SNAP protein is degraded, the fluorescence of the released probe is quenched due to aggregation. BGAN-8C was successfully employed to monitor the degradation of mODC in live cells, offering a new tool for studying protein dynamics.
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http://dx.doi.org/10.1039/d5cc00459d | DOI Listing |
Nat Chem Biol
July 2025
Department of Chemical Biology, Max Planck Institute for Medical Research, Heidelberg, Germany.
SNAP-tag is a powerful tool for labeling proteins with synthetic fluorophores in bioimaging. However, its utility in live-cell applications can be constrained by its relatively slow labeling kinetics and the limited cell permeability of its substrates. Here, we introduce improved labeling substrates and an engineered SNAP-tag for faster labeling in vitro and in live cells.
View Article and Find Full Text PDFChem Commun (Camb)
February 2025
Dalian Institute of Chemical Physics, Chinese Academy of Sciences, 457 Zhongshan Road, Dalian, 116023, China.
We developed the fluorogenic SNAP probe BGAN-8C to monitor protein degradation. It exhibited a 6-fold fluorescence enhancement upon binding with SNAP-tag. After the SNAP protein is degraded, the fluorescence of the released probe is quenched due to aggregation.
View Article and Find Full Text PDFCell Discov
June 2023
Optogenetics & Synthetic Biology Interdisciplinary Research Center, State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, China.
J Am Chem Soc
November 2022
Graduate School of Pharmaceutical Sciences, Keio University, 1-5-30 Shibakoen, Minoto-ku, Tokyo105-8512, Japan.
Fluorogenic probes for bioimaging have become essential tools for life science and medicine, and the key to their development is a precise understanding of the mechanisms available for fluorescence off/on control, such as photoinduced electron transfer (PeT) and Förster resonance energy transfer (FRET). Here we establish a new molecular design strategy to rationally develop activatable fluorescent probes, which exhibit a fluorescence off/on change in response to target biomolecules, by controlling the twisted intramolecular charge transfer (TICT) process. This approach was developed on the basis of a thorough investigation of the fluorescence quenching mechanism of -phenyl rhodamine dyes (commercially available as the QSY series) by means of time-dependent density functional theory (TD-DFT) calculations and photophysical evaluation of their derivatives.
View Article and Find Full Text PDFAngew Chem Int Ed Engl
September 2022
National Biomedical Imaging Center, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, College of Future Technology, Peking University, Yiheyuan Road No.5, Beijing, 100871, China.
Self-labeling protein tags can introduce advanced molecular motifs to specific cellular proteins. Here we introduce the third-generation covalent TMP-tag (TMP-tag3) and showcase its comparison with HaloTag and SNAP-tag. TMP-tag3 is based on a proximity-induced covalent Michael addition between an engineered Cys of E.
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