Effects of Baicalein and Chrysin on the Structure and Functional Properties of β-Lactoglobulin
Two flavonoids with similar structures, baicalein (Bai) and chrysin (Chr), were selected to investigate the interactions with β-lactoglobulin (BLG) and the influences on the structure and functional properties of BLG by multispectral methods combined with molecular docking and dynamic (MD) simulatio...
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-01-01
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| Series: | Foods |
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| Online Access: | https://www.mdpi.com/2304-8158/11/2/165 |
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| author | Ang Li Lei Chen Weijie Zhou Junhui Pan Deming Gong Guowen Zhang |
| author_facet | Ang Li Lei Chen Weijie Zhou Junhui Pan Deming Gong Guowen Zhang |
| author_sort | Ang Li |
| collection | DOAJ |
| description | Two flavonoids with similar structures, baicalein (Bai) and chrysin (Chr), were selected to investigate the interactions with β-lactoglobulin (BLG) and the influences on the structure and functional properties of BLG by multispectral methods combined with molecular docking and dynamic (MD) simulation techniques. The results of fluorescence quenching suggested that both Bai and Chr interacted with BLG to form complexes with the binding constant of the magnitude of 10<sup>5</sup> L·mol<sup>−1</sup>. The binding affinity between BLG and Bai was stronger than that of Chr due to more hydrogen bond formation in Bai–BLG binding. The existence of Bai or Chr induced a looser conformation of BLG, but Chr had a greater effect on the secondary structure of BLG. The surface hydrophobicity and free sulfhydryl group content of BLG lessened due to the presence of the two flavonoids. Molecular docking was performed at the binding site of Bai or Chr located in the surface of BLG, and hydrophobic interaction and hydrogen bond actuated the formation of the Bai/Chr–BLG complex. Molecular dynamics simulation verified that the combination of Chr and BLG decreased the stability of BLG, while Bai had little effect on it. Moreover, the foaming properties of BLG got better in the presence of the two flavonoids compounds and Bai improved its emulsification stability of the protein, but Chr had the opposite effect. This work provides a new idea for the development of novel dietary supplements using functional proteins as flavonoid delivery vectors. |
| first_indexed | 2024-03-10T01:29:53Z |
| format | Article |
| id | doaj.art-9d0d2325bc2c45f8af61d41c687030c7 |
| institution | Directory Open Access Journal |
| issn | 2304-8158 |
| language | English |
| last_indexed | 2024-03-10T01:29:53Z |
| publishDate | 2022-01-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Foods |
| spelling | doaj.art-9d0d2325bc2c45f8af61d41c687030c72023-11-23T13:44:45ZengMDPI AGFoods2304-81582022-01-0111216510.3390/foods11020165Effects of Baicalein and Chrysin on the Structure and Functional Properties of β-LactoglobulinAng Li0Lei Chen1Weijie Zhou2Junhui Pan3Deming Gong4Guowen Zhang5State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, ChinaState Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, ChinaState Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, ChinaState Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, ChinaState Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, ChinaState Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, ChinaTwo flavonoids with similar structures, baicalein (Bai) and chrysin (Chr), were selected to investigate the interactions with β-lactoglobulin (BLG) and the influences on the structure and functional properties of BLG by multispectral methods combined with molecular docking and dynamic (MD) simulation techniques. The results of fluorescence quenching suggested that both Bai and Chr interacted with BLG to form complexes with the binding constant of the magnitude of 10<sup>5</sup> L·mol<sup>−1</sup>. The binding affinity between BLG and Bai was stronger than that of Chr due to more hydrogen bond formation in Bai–BLG binding. The existence of Bai or Chr induced a looser conformation of BLG, but Chr had a greater effect on the secondary structure of BLG. The surface hydrophobicity and free sulfhydryl group content of BLG lessened due to the presence of the two flavonoids. Molecular docking was performed at the binding site of Bai or Chr located in the surface of BLG, and hydrophobic interaction and hydrogen bond actuated the formation of the Bai/Chr–BLG complex. Molecular dynamics simulation verified that the combination of Chr and BLG decreased the stability of BLG, while Bai had little effect on it. Moreover, the foaming properties of BLG got better in the presence of the two flavonoids compounds and Bai improved its emulsification stability of the protein, but Chr had the opposite effect. This work provides a new idea for the development of novel dietary supplements using functional proteins as flavonoid delivery vectors.https://www.mdpi.com/2304-8158/11/2/165baicaleinchrysinβ-lactoglobulinfunctional propertyspectrophotometrymolecular dynamics simulation |
| spellingShingle | Ang Li Lei Chen Weijie Zhou Junhui Pan Deming Gong Guowen Zhang Effects of Baicalein and Chrysin on the Structure and Functional Properties of β-Lactoglobulin Foods baicalein chrysin β-lactoglobulin functional property spectrophotometry molecular dynamics simulation |
| title | Effects of Baicalein and Chrysin on the Structure and Functional Properties of β-Lactoglobulin |
| title_full | Effects of Baicalein and Chrysin on the Structure and Functional Properties of β-Lactoglobulin |
| title_fullStr | Effects of Baicalein and Chrysin on the Structure and Functional Properties of β-Lactoglobulin |
| title_full_unstemmed | Effects of Baicalein and Chrysin on the Structure and Functional Properties of β-Lactoglobulin |
| title_short | Effects of Baicalein and Chrysin on the Structure and Functional Properties of β-Lactoglobulin |
| title_sort | effects of baicalein and chrysin on the structure and functional properties of β lactoglobulin |
| topic | baicalein chrysin β-lactoglobulin functional property spectrophotometry molecular dynamics simulation |
| url | https://www.mdpi.com/2304-8158/11/2/165 |
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