Structure-activity relationship and interaction mechanism of nine structurally similar flavonoids and α-amylase
In this study, the structure-activity relationship and interaction mechanism of nine flavonoids and porcine pancreatic α-amylase were studied through enzyme kinetics, multispectral analysis and molecular simulation. The analysis of the structure-activity relationship illustrated that hydroxylation a...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
| Published: |
Elsevier
2021-11-01
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| Series: | Journal of Functional Foods |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S1756464621003881 |
| _version_ | 1819023577506119680 |
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| author | Yiling Zhao Ming Wang Ganhui Huang |
| author_facet | Yiling Zhao Ming Wang Ganhui Huang |
| author_sort | Yiling Zhao |
| collection | DOAJ |
| description | In this study, the structure-activity relationship and interaction mechanism of nine flavonoids and porcine pancreatic α-amylase were studied through enzyme kinetics, multispectral analysis and molecular simulation. The analysis of the structure-activity relationship illustrated that hydroxylation at C4′ and C5′ position of flavonoids increased the inhibitory activity against α-amylase while the methylation at the corresponding position decreased it. According to the fluorescence quenching assay, all flavonoids could efficiently quench the intrinsic fluorescence of amylase by static mechanism and the thermodynamic parameters of representative Luteolin and Quercetin indicated the key role of hydrogen bonds and van der Waals interactions. The multispectral study suggested that the binding of flavonoids alters the secondary structure of α-amylase, leading to significant inhibition. Moreover, these findings were further confirmed by molecular docking which demonstrating the importance of hydrogen bonding and hydrophobic forces in flavonoid and porcine pancreatic α-amylase interactions. |
| first_indexed | 2024-12-21T04:41:06Z |
| format | Article |
| id | doaj.art-9d9cf7df6ce248eb912131a7caf95fe8 |
| institution | Directory Open Access Journal |
| issn | 1756-4646 |
| language | English |
| last_indexed | 2024-12-21T04:41:06Z |
| publishDate | 2021-11-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Journal of Functional Foods |
| spelling | doaj.art-9d9cf7df6ce248eb912131a7caf95fe82022-12-21T19:15:42ZengElsevierJournal of Functional Foods1756-46462021-11-0186104739Structure-activity relationship and interaction mechanism of nine structurally similar flavonoids and α-amylaseYiling Zhao0Ming Wang1Ganhui Huang2State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, PR ChinaState Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, PR ChinaCorresponding author at: 235 Nanjing East Road, Nanchang 330047, PR China.; State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, PR ChinaIn this study, the structure-activity relationship and interaction mechanism of nine flavonoids and porcine pancreatic α-amylase were studied through enzyme kinetics, multispectral analysis and molecular simulation. The analysis of the structure-activity relationship illustrated that hydroxylation at C4′ and C5′ position of flavonoids increased the inhibitory activity against α-amylase while the methylation at the corresponding position decreased it. According to the fluorescence quenching assay, all flavonoids could efficiently quench the intrinsic fluorescence of amylase by static mechanism and the thermodynamic parameters of representative Luteolin and Quercetin indicated the key role of hydrogen bonds and van der Waals interactions. The multispectral study suggested that the binding of flavonoids alters the secondary structure of α-amylase, leading to significant inhibition. Moreover, these findings were further confirmed by molecular docking which demonstrating the importance of hydrogen bonding and hydrophobic forces in flavonoid and porcine pancreatic α-amylase interactions.http://www.sciencedirect.com/science/article/pii/S1756464621003881FlavonoidsPorcine pancreatic α-amylaseStructure-activity relationshipMultispectral studyInteraction mechanism |
| spellingShingle | Yiling Zhao Ming Wang Ganhui Huang Structure-activity relationship and interaction mechanism of nine structurally similar flavonoids and α-amylase Journal of Functional Foods Flavonoids Porcine pancreatic α-amylase Structure-activity relationship Multispectral study Interaction mechanism |
| title | Structure-activity relationship and interaction mechanism of nine structurally similar flavonoids and α-amylase |
| title_full | Structure-activity relationship and interaction mechanism of nine structurally similar flavonoids and α-amylase |
| title_fullStr | Structure-activity relationship and interaction mechanism of nine structurally similar flavonoids and α-amylase |
| title_full_unstemmed | Structure-activity relationship and interaction mechanism of nine structurally similar flavonoids and α-amylase |
| title_short | Structure-activity relationship and interaction mechanism of nine structurally similar flavonoids and α-amylase |
| title_sort | structure activity relationship and interaction mechanism of nine structurally similar flavonoids and α amylase |
| topic | Flavonoids Porcine pancreatic α-amylase Structure-activity relationship Multispectral study Interaction mechanism |
| url | http://www.sciencedirect.com/science/article/pii/S1756464621003881 |
| work_keys_str_mv | AT yilingzhao structureactivityrelationshipandinteractionmechanismofninestructurallysimilarflavonoidsandaamylase AT mingwang structureactivityrelationshipandinteractionmechanismofninestructurallysimilarflavonoidsandaamylase AT ganhuihuang structureactivityrelationshipandinteractionmechanismofninestructurallysimilarflavonoidsandaamylase |