Cargando…

Interactions of Bromocarbazoles with Human Serum Albumin Using Spectroscopic Methods

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 spectrosco...

Descripción completa

Detalles Bibliográficos
Autores principales: Yan, Xiaodan, Yuan, Dongjie, Pan, Dandan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6321538/
https://www.ncbi.nlm.nih.gov/pubmed/30487451
http://dx.doi.org/10.3390/molecules23123120
_version_ 1783385466422165504
author Yan, Xiaodan
Yuan, Dongjie
Pan, Dandan
author_facet Yan, Xiaodan
Yuan, Dongjie
Pan, Dandan
author_sort Yan, Xiaodan
collection PubMed
description 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.
format Online
Article
Text
id pubmed-6321538
institution National Center for Biotechnology Information
language English
publishDate 2018
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-63215382019-01-14 Interactions of Bromocarbazoles with Human Serum Albumin Using Spectroscopic Methods Yan, Xiaodan Yuan, Dongjie Pan, Dandan Molecules Article 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. MDPI 2018-11-28 /pmc/articles/PMC6321538/ /pubmed/30487451 http://dx.doi.org/10.3390/molecules23123120 Text en © 2018 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Yan, Xiaodan
Yuan, Dongjie
Pan, Dandan
Interactions of Bromocarbazoles with Human Serum Albumin Using Spectroscopic Methods
title Interactions of Bromocarbazoles with Human Serum Albumin Using Spectroscopic Methods
title_full Interactions of Bromocarbazoles with Human Serum Albumin Using Spectroscopic Methods
title_fullStr Interactions of Bromocarbazoles with Human Serum Albumin Using Spectroscopic Methods
title_full_unstemmed Interactions of Bromocarbazoles with Human Serum Albumin Using Spectroscopic Methods
title_short Interactions of Bromocarbazoles with Human Serum Albumin Using Spectroscopic Methods
title_sort interactions of bromocarbazoles with human serum albumin using spectroscopic methods
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6321538/
https://www.ncbi.nlm.nih.gov/pubmed/30487451
http://dx.doi.org/10.3390/molecules23123120
work_keys_str_mv AT yanxiaodan interactionsofbromocarbazoleswithhumanserumalbuminusingspectroscopicmethods
AT yuandongjie interactionsofbromocarbazoleswithhumanserumalbuminusingspectroscopicmethods
AT pandandan interactionsofbromocarbazoleswithhumanserumalbuminusingspectroscopicmethods