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

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© The Author(s) 2024

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 3 — a Schematic illustration of the binding domain between NIR-II chromophores and HSA. b Brightness (mean ± SD, n = 10 independent samples per group) and c gel electrophoresis analysis (n = 4 independent experiment) of the binding ability between Et-1080, CO-1080, FD-1080 chromophores and HSA, DI, DII, DIII. d Comparison of the covalent binding ability between three dyes and HSA, DI, DII, DIII. e High-resolution mass spectrometry of the DIII, DIII@Et-1080, DIII@CO-1080, and DIII@FD-1080. f Gel electrophoresis results of CO-1080 and CO-1080@Cys binding to HSA (n = 4 independent experiment). g Mass spectra of the CO-1080 and CO-1080@Cys obtained in a catalyst-free condition with a molar ratio of CO-1080 to Cys at 1:1(Cys: L-cysteine). h Reaction diagram showing CO-1080 with Cys and HSA (or DIII). Protein structures were generated by the Protein Data Bank (PDB). Source data are provided as a Source Data file.