Effect of Sugarcane Polyphenol Extract on α-Amylase Inhibition and Mechanism Exploration
Although α-amylase is crucial for postprandial glucose control, existing inhibitors present various side effects, necessitating the exploration of natural alternatives. The ability of sugarcane polyphenol (SP) to inhibit α-amylase remains unclear. This study assessed the inhibitory activity of SP vi...
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| Format: | Article |
| Language: | English |
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MDPI AG
2025-06-01
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| Series: | Foods |
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| Online Access: | https://www.mdpi.com/2304-8158/14/13/2174 |
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| author | Yumei Wang Jiulong An Shenghong Yao Chengfeng Zhang Yanv Zhou Lu Li He Li |
| author_facet | Yumei Wang Jiulong An Shenghong Yao Chengfeng Zhang Yanv Zhou Lu Li He Li |
| author_sort | Yumei Wang |
| collection | DOAJ |
| description | Although α-amylase is crucial for postprandial glucose control, existing inhibitors present various side effects, necessitating the exploration of natural alternatives. The ability of sugarcane polyphenol (SP) to inhibit α-amylase remains unclear. This study assessed the inhibitory activity of SP via in vitro assays, circular dichroism (CD), fluorescence quenching, and stability analysis, while the mechanism of action was elucidated using molecular docking and molecular dynamics (MD). The results showed that the IC<sub>50</sub> of the SP was 0.841 ± 0.029 mg/mL, with proanthocyanidin-B1 (PC-B1) presenting the most potent effect (IC<sub>50</sub> = 0.504 ± 0.019 mg/mL). CD and barycentric mean (BCM) analysis indicated that the complexes might limit substrate binding. The mechanistic assessment showed that the polyphenols bonded to the active enzyme pockets to form stable complexes with reduced key residue fluctuations. In conclusion, SP, especially PC-B1, effectively inhibited α-amylase activity via structural regulation and molecular interactions, providing a theoretical basis for developing natural hypoglycemic agents. |
| format | Article |
| id | doaj-art-8105bfc2ab4f498d809de75d7c2527d5 |
| institution | DOAJ |
| issn | 2304-8158 |
| language | English |
| publishDate | 2025-06-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Foods |
| spelling | doaj-art-8105bfc2ab4f498d809de75d7c2527d52025-08-20T03:16:55ZengMDPI AGFoods2304-81582025-06-011413217410.3390/foods14132174Effect of Sugarcane Polyphenol Extract on α-Amylase Inhibition and Mechanism ExplorationYumei Wang0Jiulong An1Shenghong Yao2Chengfeng Zhang3Yanv Zhou4Lu Li5He Li6Key Laboratory of Geriatric Nutrition and Health, Beijing Technology and Business University, Ministry of Education, Beijing 100048, ChinaKey Laboratory of Geriatric Nutrition and Health, Beijing Technology and Business University, Ministry of Education, Beijing 100048, ChinaKey Laboratory of Geriatric Nutrition and Health, Beijing Technology and Business University, Ministry of Education, Beijing 100048, ChinaThe Product Makers Co., Ltd., Shanghai 200444, ChinaThe Product Makers Co., Ltd., Shanghai 200444, ChinaKey Laboratory of Geriatric Nutrition and Health, Beijing Technology and Business University, Ministry of Education, Beijing 100048, ChinaKey Laboratory of Geriatric Nutrition and Health, Beijing Technology and Business University, Ministry of Education, Beijing 100048, ChinaAlthough α-amylase is crucial for postprandial glucose control, existing inhibitors present various side effects, necessitating the exploration of natural alternatives. The ability of sugarcane polyphenol (SP) to inhibit α-amylase remains unclear. This study assessed the inhibitory activity of SP via in vitro assays, circular dichroism (CD), fluorescence quenching, and stability analysis, while the mechanism of action was elucidated using molecular docking and molecular dynamics (MD). The results showed that the IC<sub>50</sub> of the SP was 0.841 ± 0.029 mg/mL, with proanthocyanidin-B1 (PC-B1) presenting the most potent effect (IC<sub>50</sub> = 0.504 ± 0.019 mg/mL). CD and barycentric mean (BCM) analysis indicated that the complexes might limit substrate binding. The mechanistic assessment showed that the polyphenols bonded to the active enzyme pockets to form stable complexes with reduced key residue fluctuations. In conclusion, SP, especially PC-B1, effectively inhibited α-amylase activity via structural regulation and molecular interactions, providing a theoretical basis for developing natural hypoglycemic agents.https://www.mdpi.com/2304-8158/14/13/2174sugarcane polyphenolsproanthocyanidin-B1chlorogenic acidα-amylase inhibitionstability analysismolecular dynamics |
| spellingShingle | Yumei Wang Jiulong An Shenghong Yao Chengfeng Zhang Yanv Zhou Lu Li He Li Effect of Sugarcane Polyphenol Extract on α-Amylase Inhibition and Mechanism Exploration Foods sugarcane polyphenols proanthocyanidin-B1 chlorogenic acid α-amylase inhibition stability analysis molecular dynamics |
| title | Effect of Sugarcane Polyphenol Extract on α-Amylase Inhibition and Mechanism Exploration |
| title_full | Effect of Sugarcane Polyphenol Extract on α-Amylase Inhibition and Mechanism Exploration |
| title_fullStr | Effect of Sugarcane Polyphenol Extract on α-Amylase Inhibition and Mechanism Exploration |
| title_full_unstemmed | Effect of Sugarcane Polyphenol Extract on α-Amylase Inhibition and Mechanism Exploration |
| title_short | Effect of Sugarcane Polyphenol Extract on α-Amylase Inhibition and Mechanism Exploration |
| title_sort | effect of sugarcane polyphenol extract on α amylase inhibition and mechanism exploration |
| topic | sugarcane polyphenols proanthocyanidin-B1 chlorogenic acid α-amylase inhibition stability analysis molecular dynamics |
| url | https://www.mdpi.com/2304-8158/14/13/2174 |
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