Fig. 2: Elucidation of the albumin-fluorophore binding mechanism. | Nature Communications

Fig. 2: Elucidation of the albumin-fluorophore binding mechanism.

From: A pocket-escaping design to prevent the common interference with near-infrared fluorescent probes in vivo

Fig. 2

a The illustration of “transplanted” TICT dyes. b Chemical structures of NC, BNC, BNCQ, BNCN, BNCY, and BNCE. c Fluorescence of BNC, BNCQ, and BNCN in PBS solution (pH 7.4, 10 mM) under a 365 nm excitation. d DFT optimized molecular orbital plots (LUMO and HOMO) of BNC, BNCQ, BNCN, and BNCN-90°. e Concentration-dependent fluorescence changes of NC, BNC, BNCQ, BNCN, BNCY, and BNCE with the addition of albumin (10−600 µM) in PBS solution (pH 7.4, 10 mM) at room temperature. f Fold changes (from white to blue) for NC, BNCN, BNCY, and BNCE in 10 µM albumin with different concentration of inhibitors. Con. indicates the concentration of the inhibitors. 1, 0 µM; 2, 50 µM; 3, 100 µM; 4, 150 µM; 5, 200 µM; 6, 250 µM. g The conformation of albumin and NC. h The scheme of “pocket capture” for albumin to TICT dyes. F0 and F are the fluorescence intensity at the maximum emission wavelength without and with the presence of analyte, respectively. Source data for Fig. 2e, f are provided as a Source Data file.

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