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. 2024 Apr 2;15:2845. doi: 10.1038/s41467-024-47063-4

Fig. 2. Optimization of biomimetic NIR-II fluorescent proteins through chromophore selection.

Fig. 2

a Chemical structure and b NIR-II brightness of the Et-1080, CO-1080, and FD-1080 chromophores (n = 5 independent samples per group). c-d NIR-II brightness and e fluorescence enhancement effect of HSA@Et-1080, HSA@CO-1080, and HSA@FD-1080 FPs (n = 15 independent samples per group). Theoretical simulation of HSA binding to f Et-1080, g CO-1080, and h FD-1080 chromophores by gliding docking mode. Comparison of i docking score and j binding energy between HSA and three chromophores, including Et-1080, CO-1080, and FD-1080 chromophores. k Gel electrophoresis analysis of the HSA@Et-1080, HSA@CO-1080, and HSA@FD-1080 FPs (n = 4 independent experiment). l High-resolution mass spectrometry of the free HSA, HSA@Et-1080, HSA@CO-1080, and HSA@FD-1080. Protein structures were generated by the Protein Data Bank (PDB). Source data are provided as a Source Data file.