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Open AccessArticle

Interactions of Bromocarbazoles with Human Serum Albumin Using Spectroscopic Methods

1
School of Management, Hefei University of Technology, Hefei 230009, China
2
Anhui Public Inspection Institute Co., Ltd., Hefei 230051, China
3
College of Resources and Environment, Anhui Agricultural University, No. 130 Chang jiang West Road, Hefei 230036, China
*
Author to whom correspondence should be addressed.
Molecules 2018, 23(12), 3120; https://doi.org/10.3390/molecules23123120
Received: 7 November 2018 / Revised: 26 November 2018 / Accepted: 26 November 2018 / Published: 28 November 2018
The 1,3,6,8-tetrabromocarbazole and 3-bromocarbazole have attracted great attention in the ecotoxicology field recently as hazardous environmental contaminants. In this study, the quenching mechanism of these two substances binding with human serum albumin (HSA) has been investigated with spectroscopic methods. Through fluorescence quenching and binding site experiments with steady-state fluorescence and UV-Vis spectra, the intrinsic fluorescence of HSA quenched by 1,3,6,8-tetrabromocarbazole and 3-bromocarbazole both in static process, are activated by binding to site II (subdomain IIIA) of the HSA. In addition, it was not only found that the conformation and secondary structure of the proteins changes, but also that their spontaneous binding processes were driven by electrostatic interactions as well as hydrophobic forces for HSA-1,3,6,8-tetrabromocarbazole, and by typical hydrophobic forces for HSA-3-bromocarbazole. The above studies are beneficial to enhance our understanding of the ecotoxicology and environmental behaviors of halogenated carbazoles. View Full-Text
Keywords: 1,3,6,8-tetrabromocarbazole; 3-bromocarbazole; human serum albumin; spectroscopic method; site II (subdomain IIIA) 1,3,6,8-tetrabromocarbazole; 3-bromocarbazole; human serum albumin; spectroscopic method; site II (subdomain IIIA)
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Yan, X.; Yuan, D.; Pan, D. Interactions of Bromocarbazoles with Human Serum Albumin Using Spectroscopic Methods. Molecules 2018, 23, 3120.

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