A deep understanding of the molecular interactions of carbon nanodots with biomacromolecules is essential for wider applications of carbon nanodots both in vitro and in vivo. Herein, nitrogen and sulfur co-doped carbon dots (N,S-CDs) with a quantum yield of 16% were synthesized by a 1-step hydrothermal method. The N,S-CDs exhibited a good dispersion, with a graphite-like structure, along with the fluorescence lifetime of approximately 7.50 ns. Findings showed that the fluorescence of the N,S-CDs was effectively quenched by bovine hemoglobin as a result of the static fluorescence quenching. The mentioned quenching mechanism was investigated by the Stern-Volmer equation, temperature-dependent quenching, and fluorescence lifetime measurements. The binding constants, number of binding sites, and the binding average distance between the energy donor N,S-CDs and acceptor bovine hemoglobin were calculated as well. These findings will provide for valuable insights on the future bioapplications of N,S-CDs.
Nitrogen and sulfur co-doped carbon nanodots toward bovine hemoglobin: A fluorescence quenching mechanism investigation / Wang, J.; Xiang, X.; Milcovich, G.; Chen, J.; Chen, C.; Feng, J.; Hudson, S. P.; Weng, X.; Ruan, Y.. - In: JOURNAL OF MOLECULAR RECOGNITION. - ISSN 0952-3499. - 32:2(2019), pp. 1-9. [10.1002/jmr.2761]
Nitrogen and sulfur co-doped carbon nanodots toward bovine hemoglobin: A fluorescence quenching mechanism investigation
Milcovich G.;
2019
Abstract
A deep understanding of the molecular interactions of carbon nanodots with biomacromolecules is essential for wider applications of carbon nanodots both in vitro and in vivo. Herein, nitrogen and sulfur co-doped carbon dots (N,S-CDs) with a quantum yield of 16% were synthesized by a 1-step hydrothermal method. The N,S-CDs exhibited a good dispersion, with a graphite-like structure, along with the fluorescence lifetime of approximately 7.50 ns. Findings showed that the fluorescence of the N,S-CDs was effectively quenched by bovine hemoglobin as a result of the static fluorescence quenching. The mentioned quenching mechanism was investigated by the Stern-Volmer equation, temperature-dependent quenching, and fluorescence lifetime measurements. The binding constants, number of binding sites, and the binding average distance between the energy donor N,S-CDs and acceptor bovine hemoglobin were calculated as well. These findings will provide for valuable insights on the future bioapplications of N,S-CDs.File | Dimensione | Formato | |
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