Fig. 2: Design and characterization of ESR. | Nature Communications

Fig. 2: Design and characterization of ESR.

From: Non-invasive in vivo monitoring of PROTAC-mediated protein degradation using an environment-sensitive reporter

Fig. 2

a Chemical structures of classical environment-sensitive fluorophores. b Polarity of different solvents. c Optical properties of classical fluorophores (2 μM) in various solvents (Experiments were repeated three times). d Correlation between different solvent polarities and fluorophores fluorescent intensity. Pearson r and P values were derived using a simple linear regression model. The error band shows the 95% confidence intervals of the fitted line by two-tailed Student t-test analysis. e Schematic illustration of JQ1-n-NR (n = 1, 2, 3) for quantitatively imaging BRD4 levels. f The cellular thermal shift assay (CETSA) for the binding of different groups (DMSO, JQ1 ( + ), NR, and JQ1-1-NR (10 μM)) to BRD4 protein in 4T1 cell lysate. (Experiments were repeated three times). g Fluorescence intensity ratios of JQ1-n-NR (10 μM) incubated with different concentrations of BRD4 protein (0–12 μM) (Data are presented as mean value ± SD, experiments were repeated three times). h The linear curves obtained by the fluorescence ratios of JQ1-n-NR (10 μM) with BRD4 protein (0-8 μM) (Data are presented as mean value ± SD, experiments were repeated three times). Source data are provided as a Source Data file.

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