Cargando…

Characterization of Soybean Protein Isolate-Food Polyphenol Interaction via Virtual Screening and Experimental Studies

(1) Background: Protein–polyphenol interactions have been widely studied regarding their influence on the properties of both protein and the ligands. As an important protein material in the food industry, soybean protein isolate (SPI) experiences interesting changes through polyphenols binding. (2)...

Descripción completa

Detalles Bibliográficos
Autores principales: Ao, Le, Liu, Panhang, Wu, Annan, Zhao, Jing, Hu, Xiaosong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8625844/
https://www.ncbi.nlm.nih.gov/pubmed/34829094
http://dx.doi.org/10.3390/foods10112813
_version_ 1784606521101910016
author Ao, Le
Liu, Panhang
Wu, Annan
Zhao, Jing
Hu, Xiaosong
author_facet Ao, Le
Liu, Panhang
Wu, Annan
Zhao, Jing
Hu, Xiaosong
author_sort Ao, Le
collection PubMed
description (1) Background: Protein–polyphenol interactions have been widely studied regarding their influence on the properties of both protein and the ligands. As an important protein material in the food industry, soybean protein isolate (SPI) experiences interesting changes through polyphenols binding. (2) Methods: In this study, a molecular docking and virtual screening method was established to evaluate the SPI–polyphenol interaction. A compound library composed of 33 commonly found food source polyphenols was used in virtual screening. The binding capacity of top-ranking polyphenols (rutin, procyanidin, cyanidin chloride, quercetin) was validated and compared by fluorescence assays. (3) Results: Four out of five top-ranking polyphenols in virtual screening were flavonoids, while phenolic acids exhibit low binding capacity. Hydrogen bonding and hydrophobic interactions were found to be dominant interactions involved in soybean protein–polyphenol binding. Cyanidin chloride exhibited the highest apparent binding constant (Ka), which was followed by quercetin, procyanidin, and rutin. Unlike others, procyanidin addition perturbed a red shift of SPI fluorescence, indicating a slight conformational change of SPI. (4) Conclusions: These results suggest that the pattern of SPI–polyphenol interaction is highly dependent on the detailed structure of polyphenols, which have important implications in uncovering the binding mechanism of SPI–polyphenol interaction.
format Online
Article
Text
id pubmed-8625844
institution National Center for Biotechnology Information
language English
publishDate 2021
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-86258442021-11-27 Characterization of Soybean Protein Isolate-Food Polyphenol Interaction via Virtual Screening and Experimental Studies Ao, Le Liu, Panhang Wu, Annan Zhao, Jing Hu, Xiaosong Foods Article (1) Background: Protein–polyphenol interactions have been widely studied regarding their influence on the properties of both protein and the ligands. As an important protein material in the food industry, soybean protein isolate (SPI) experiences interesting changes through polyphenols binding. (2) Methods: In this study, a molecular docking and virtual screening method was established to evaluate the SPI–polyphenol interaction. A compound library composed of 33 commonly found food source polyphenols was used in virtual screening. The binding capacity of top-ranking polyphenols (rutin, procyanidin, cyanidin chloride, quercetin) was validated and compared by fluorescence assays. (3) Results: Four out of five top-ranking polyphenols in virtual screening were flavonoids, while phenolic acids exhibit low binding capacity. Hydrogen bonding and hydrophobic interactions were found to be dominant interactions involved in soybean protein–polyphenol binding. Cyanidin chloride exhibited the highest apparent binding constant (Ka), which was followed by quercetin, procyanidin, and rutin. Unlike others, procyanidin addition perturbed a red shift of SPI fluorescence, indicating a slight conformational change of SPI. (4) Conclusions: These results suggest that the pattern of SPI–polyphenol interaction is highly dependent on the detailed structure of polyphenols, which have important implications in uncovering the binding mechanism of SPI–polyphenol interaction. MDPI 2021-11-16 /pmc/articles/PMC8625844/ /pubmed/34829094 http://dx.doi.org/10.3390/foods10112813 Text en © 2021 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
Ao, Le
Liu, Panhang
Wu, Annan
Zhao, Jing
Hu, Xiaosong
Characterization of Soybean Protein Isolate-Food Polyphenol Interaction via Virtual Screening and Experimental Studies
title Characterization of Soybean Protein Isolate-Food Polyphenol Interaction via Virtual Screening and Experimental Studies
title_full Characterization of Soybean Protein Isolate-Food Polyphenol Interaction via Virtual Screening and Experimental Studies
title_fullStr Characterization of Soybean Protein Isolate-Food Polyphenol Interaction via Virtual Screening and Experimental Studies
title_full_unstemmed Characterization of Soybean Protein Isolate-Food Polyphenol Interaction via Virtual Screening and Experimental Studies
title_short Characterization of Soybean Protein Isolate-Food Polyphenol Interaction via Virtual Screening and Experimental Studies
title_sort characterization of soybean protein isolate-food polyphenol interaction via virtual screening and experimental studies
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8625844/
https://www.ncbi.nlm.nih.gov/pubmed/34829094
http://dx.doi.org/10.3390/foods10112813
work_keys_str_mv AT aole characterizationofsoybeanproteinisolatefoodpolyphenolinteractionviavirtualscreeningandexperimentalstudies
AT liupanhang characterizationofsoybeanproteinisolatefoodpolyphenolinteractionviavirtualscreeningandexperimentalstudies
AT wuannan characterizationofsoybeanproteinisolatefoodpolyphenolinteractionviavirtualscreeningandexperimentalstudies
AT zhaojing characterizationofsoybeanproteinisolatefoodpolyphenolinteractionviavirtualscreeningandexperimentalstudies
AT huxiaosong characterizationofsoybeanproteinisolatefoodpolyphenolinteractionviavirtualscreeningandexperimentalstudies