Cargando…
Molecular Insight into the Binding of Astilbin with Human Serum Albumin and Its Effect on Antioxidant Characteristics of Astilbin
Astilbin is a dihydroflavonol glycoside identified in many natural plants and functional food with promising biological activities which is used as an antioxidant in the pharmaceutical and food fields. This work investigated the interaction between astilbin and human serum albumin (HSA) and their ef...
Autores principales: | , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9321622/ https://www.ncbi.nlm.nih.gov/pubmed/35889360 http://dx.doi.org/10.3390/molecules27144487 |
_version_ | 1784756093077946368 |
---|---|
author | Han, Xiangyu Sun, Jing Niu, Tianmei Mao, Beibei Gao, Shijie Zhao, Pan Sun, Linlin |
author_facet | Han, Xiangyu Sun, Jing Niu, Tianmei Mao, Beibei Gao, Shijie Zhao, Pan Sun, Linlin |
author_sort | Han, Xiangyu |
collection | PubMed |
description | Astilbin is a dihydroflavonol glycoside identified in many natural plants and functional food with promising biological activities which is used as an antioxidant in the pharmaceutical and food fields. This work investigated the interaction between astilbin and human serum albumin (HSA) and their effects on the antioxidant activity of astilbin by multi-spectroscopic and molecular modeling studies. The experimental results show that astilbin quenches the fluorescence emission of HSA through a static quenching mechanism. Astilbin and HSA prefer to bind at the Site Ⅰ position, which is mainly maintained by electrostatic force, hydrophobic and hydrogen bonding interactions. Multi-spectroscopic and MD results indicate that the secondary structure of HSA could be changed because of the interaction of astilbin with HSA. DPPH radical scavenging assay shows that the presence of HSA reduces the antioxidant capacity of astilbin. The explication of astilbin–HSA binding mechanism will provide insights into clinical use and resource development of astilbin in food and pharmaceutical industries. |
format | Online Article Text |
id | pubmed-9321622 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-93216222022-07-27 Molecular Insight into the Binding of Astilbin with Human Serum Albumin and Its Effect on Antioxidant Characteristics of Astilbin Han, Xiangyu Sun, Jing Niu, Tianmei Mao, Beibei Gao, Shijie Zhao, Pan Sun, Linlin Molecules Article Astilbin is a dihydroflavonol glycoside identified in many natural plants and functional food with promising biological activities which is used as an antioxidant in the pharmaceutical and food fields. This work investigated the interaction between astilbin and human serum albumin (HSA) and their effects on the antioxidant activity of astilbin by multi-spectroscopic and molecular modeling studies. The experimental results show that astilbin quenches the fluorescence emission of HSA through a static quenching mechanism. Astilbin and HSA prefer to bind at the Site Ⅰ position, which is mainly maintained by electrostatic force, hydrophobic and hydrogen bonding interactions. Multi-spectroscopic and MD results indicate that the secondary structure of HSA could be changed because of the interaction of astilbin with HSA. DPPH radical scavenging assay shows that the presence of HSA reduces the antioxidant capacity of astilbin. The explication of astilbin–HSA binding mechanism will provide insights into clinical use and resource development of astilbin in food and pharmaceutical industries. MDPI 2022-07-13 /pmc/articles/PMC9321622/ /pubmed/35889360 http://dx.doi.org/10.3390/molecules27144487 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/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 (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Han, Xiangyu Sun, Jing Niu, Tianmei Mao, Beibei Gao, Shijie Zhao, Pan Sun, Linlin Molecular Insight into the Binding of Astilbin with Human Serum Albumin and Its Effect on Antioxidant Characteristics of Astilbin |
title | Molecular Insight into the Binding of Astilbin with Human Serum Albumin and Its Effect on Antioxidant Characteristics of Astilbin |
title_full | Molecular Insight into the Binding of Astilbin with Human Serum Albumin and Its Effect on Antioxidant Characteristics of Astilbin |
title_fullStr | Molecular Insight into the Binding of Astilbin with Human Serum Albumin and Its Effect on Antioxidant Characteristics of Astilbin |
title_full_unstemmed | Molecular Insight into the Binding of Astilbin with Human Serum Albumin and Its Effect on Antioxidant Characteristics of Astilbin |
title_short | Molecular Insight into the Binding of Astilbin with Human Serum Albumin and Its Effect on Antioxidant Characteristics of Astilbin |
title_sort | molecular insight into the binding of astilbin with human serum albumin and its effect on antioxidant characteristics of astilbin |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9321622/ https://www.ncbi.nlm.nih.gov/pubmed/35889360 http://dx.doi.org/10.3390/molecules27144487 |
work_keys_str_mv | AT hanxiangyu molecularinsightintothebindingofastilbinwithhumanserumalbuminanditseffectonantioxidantcharacteristicsofastilbin AT sunjing molecularinsightintothebindingofastilbinwithhumanserumalbuminanditseffectonantioxidantcharacteristicsofastilbin AT niutianmei molecularinsightintothebindingofastilbinwithhumanserumalbuminanditseffectonantioxidantcharacteristicsofastilbin AT maobeibei molecularinsightintothebindingofastilbinwithhumanserumalbuminanditseffectonantioxidantcharacteristicsofastilbin AT gaoshijie molecularinsightintothebindingofastilbinwithhumanserumalbuminanditseffectonantioxidantcharacteristicsofastilbin AT zhaopan molecularinsightintothebindingofastilbinwithhumanserumalbuminanditseffectonantioxidantcharacteristicsofastilbin AT sunlinlin molecularinsightintothebindingofastilbinwithhumanserumalbuminanditseffectonantioxidantcharacteristicsofastilbin |