Fluorescence Spectroscopic Investigation of Competitive Interactions between Quercetin and Aflatoxin B<sub>1</sub> for Binding to Human Serum Albumin
Aflatoxin B<sub>1</sub> (AFB<sub>1</sub>) is a highly toxic mycotoxin found worldwide in cereals, food, and animal feeds. AFB<sub>1</sub> binds to human serum albumin (HSA) with high affinity. In previous experiments, it has been revealed that reducing the binding...
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doaj-6a6909171af547c1b3f287947ba05dcc2020-11-25T00:52:34ZengMDPI AGToxins2072-66512019-04-0111421410.3390/toxins11040214toxins11040214Fluorescence Spectroscopic Investigation of Competitive Interactions between Quercetin and Aflatoxin B<sub>1</sub> for Binding to Human Serum AlbuminHongxia Tan0Lu Chen1Liang Ma2Shuang Liu3Hongyuan Zhou4Yuhao Zhang5Ting Guo6Wei Liu7Hongjie Dai8Yong Yu9College of Food Science, Southwest University, Chongqing 400715, ChinaCollege of Food Science, Southwest University, Chongqing 400715, ChinaCollege of Food Science, Southwest University, Chongqing 400715, ChinaCollege of Food Science, Southwest University, Chongqing 400715, ChinaCollege of Food Science, Southwest University, Chongqing 400715, ChinaCollege of Food Science, Southwest University, Chongqing 400715, ChinaCollege of Food Science, Southwest University, Chongqing 400715, ChinaCollege of Food Science, Southwest University, Chongqing 400715, ChinaCollege of Food Science, Southwest University, Chongqing 400715, ChinaCollege of Food Science, Southwest University, Chongqing 400715, ChinaAflatoxin B<sub>1</sub> (AFB<sub>1</sub>) is a highly toxic mycotoxin found worldwide in cereals, food, and animal feeds. AFB<sub>1</sub> binds to human serum albumin (HSA) with high affinity. In previous experiments, it has been revealed that reducing the binding rate of AFB<sub>1</sub> with HSA could speed up the elimination rate of AFB<sub>1</sub>. Therefore, we examined the ability of quercetin to compete with AFB<sub>1</sub> for binding HSA by fluorescence spectroscopy, synchronous spectroscopy, ultrafiltration studies, etc. It was shown that AFB<sub>1</sub> and quercetin bind to HSA in the same Sudlow site I (subdomain IIA), and the binding constant (K<sub>a</sub>) of the quercetin-HSA complex is significantly stronger than the complex of AFB<sub>1</sub>-HSA. Our data in this experiment showed that quercetin is able to remove the AFB<sub>1</sub> from HSA and reduce its bound fraction. This exploratory work may be of significance for studies in the future regarding decreasing its bound fraction and then increasing its elimination rate for detoxification. This exploratory study may initiate future epidemiological research designs to obtain further in vivo evidence of the long-term (potential protective) effects of competing substances on human patients.https://www.mdpi.com/2072-6651/11/4/214aflatoxin B<sub>1</sub>quercetinhuman serum albumincompetitive interactionfluorescence spectroscopy |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Hongxia Tan Lu Chen Liang Ma Shuang Liu Hongyuan Zhou Yuhao Zhang Ting Guo Wei Liu Hongjie Dai Yong Yu |
spellingShingle |
Hongxia Tan Lu Chen Liang Ma Shuang Liu Hongyuan Zhou Yuhao Zhang Ting Guo Wei Liu Hongjie Dai Yong Yu Fluorescence Spectroscopic Investigation of Competitive Interactions between Quercetin and Aflatoxin B<sub>1</sub> for Binding to Human Serum Albumin Toxins aflatoxin B<sub>1</sub> quercetin human serum albumin competitive interaction fluorescence spectroscopy |
author_facet |
Hongxia Tan Lu Chen Liang Ma Shuang Liu Hongyuan Zhou Yuhao Zhang Ting Guo Wei Liu Hongjie Dai Yong Yu |
author_sort |
Hongxia Tan |
title |
Fluorescence Spectroscopic Investigation of Competitive Interactions between Quercetin and Aflatoxin B<sub>1</sub> for Binding to Human Serum Albumin |
title_short |
Fluorescence Spectroscopic Investigation of Competitive Interactions between Quercetin and Aflatoxin B<sub>1</sub> for Binding to Human Serum Albumin |
title_full |
Fluorescence Spectroscopic Investigation of Competitive Interactions between Quercetin and Aflatoxin B<sub>1</sub> for Binding to Human Serum Albumin |
title_fullStr |
Fluorescence Spectroscopic Investigation of Competitive Interactions between Quercetin and Aflatoxin B<sub>1</sub> for Binding to Human Serum Albumin |
title_full_unstemmed |
Fluorescence Spectroscopic Investigation of Competitive Interactions between Quercetin and Aflatoxin B<sub>1</sub> for Binding to Human Serum Albumin |
title_sort |
fluorescence spectroscopic investigation of competitive interactions between quercetin and aflatoxin b<sub>1</sub> for binding to human serum albumin |
publisher |
MDPI AG |
series |
Toxins |
issn |
2072-6651 |
publishDate |
2019-04-01 |
description |
Aflatoxin B<sub>1</sub> (AFB<sub>1</sub>) is a highly toxic mycotoxin found worldwide in cereals, food, and animal feeds. AFB<sub>1</sub> binds to human serum albumin (HSA) with high affinity. In previous experiments, it has been revealed that reducing the binding rate of AFB<sub>1</sub> with HSA could speed up the elimination rate of AFB<sub>1</sub>. Therefore, we examined the ability of quercetin to compete with AFB<sub>1</sub> for binding HSA by fluorescence spectroscopy, synchronous spectroscopy, ultrafiltration studies, etc. It was shown that AFB<sub>1</sub> and quercetin bind to HSA in the same Sudlow site I (subdomain IIA), and the binding constant (K<sub>a</sub>) of the quercetin-HSA complex is significantly stronger than the complex of AFB<sub>1</sub>-HSA. Our data in this experiment showed that quercetin is able to remove the AFB<sub>1</sub> from HSA and reduce its bound fraction. This exploratory work may be of significance for studies in the future regarding decreasing its bound fraction and then increasing its elimination rate for detoxification. This exploratory study may initiate future epidemiological research designs to obtain further in vivo evidence of the long-term (potential protective) effects of competing substances on human patients. |
topic |
aflatoxin B<sub>1</sub> quercetin human serum albumin competitive interaction fluorescence spectroscopy |
url |
https://www.mdpi.com/2072-6651/11/4/214 |
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