Related Experiment Video
Updated: Aug 12, 2025

Dual-Color Fluorescence Cross-Correlation Spectroscopy to Study Protein-Protein Interaction and Protein Dynamics in Live Cells
Published on: December 11, 2021
A "dual-key-and-lock" ratiometric fluorescent probe with biocompatibility and selectivity for imaging vicinal dithiol
Guang-Yue Zou1, Yun Wen1, Fan Bi1
1Research Center for Analytical Sciences, Department of Chemistry, College of Sciences, Northeastern University, Box 332, Shenyang 110819, China. chenshuai@mail.neu.edu.cn.
Abstract:
TMR-TPE, a ratiometric fluorescent probe, was reported for the imaging of vicinal dithiol proteins (VDPs) in living cells. Profiting from the "dual-key-and-lock" design, TMR-TPE solves the toxicity problem of VDP probes (98% cell viability at 50 μM) and avoids the interference of small thiols (up to 10 mM GSH). The change of VDPs during drug-induced liver injury was monitored for the first time using TMR-TPE.
Related Concept Videos
Labeling DNA Probes
Radioisotopes, fluorophores, or small molecule binding partners like biotin or digoxigenin, are the most widely used reporter tags for labeling DNA probes. These labels can be attached to the probe DNA molecule via...
Protein Dynamics in Living Cells
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...

