Nitrogen and sulfur co‐doped carbon nanodots toward bovine hemoglobin: A fluorescence quenching mechanism investigation. Issue 2 (22nd August 2018)

• Record Type: Journal Article
• Authors: Wang, Jiajun; Xiang, Xueqing; Milcovich, Gesmi; Chen, Jingru; Chen, Chao; Feng, Jiuju; Hudson, Sarah P.; Weng, Xuexiang; Ruan, Yongming
• Is Part Of: Journal of molecular recognition. Volume 32:Issue 2(2019)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2018-08-22
• Subjects: bovine hemoglobin -- fluorescence -- nitrogen and sulfur co‐doped carbon dots -- quenching mechanism; Molecular recognition -- Periodicals; Models, Molecular -- Periodicals; Molecular Conformation -- Periodicals; Molecular Sequence Data -- Periodicals; Molecular Structure -- Periodicals; Carrier Proteins -- Periodicals; 572.8
• DOI: 10.1002/jmr.2761
• Languages: English
• ISSNs: 0952-3499

Abstract

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. Abstract : The fluorescence quenching mechanism of nitrogen and sulfur co‐doped carbon dots toward hemoglobin 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 were calculated as well.