Inhibitory Effect of Naringin on α-Glucosidase and Its Mechanism
To investigate the inhibitory activity and mechanism of naringin on α-glucosidase, the inhibition effect, type, and molecular mechanism of naringin on α-glucosidase were investigated by integrative analysis of enzyme kinetics, fluorescence spectroscopy and molecular docking simulation. The results s...
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| Format: | Article |
| Language: | zho |
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The editorial department of Science and Technology of Food Industry
2022-04-01
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| Series: | Shipin gongye ke-ji |
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| Online Access: | http://www.spgykj.com/cn/article/doi/10.13386/j.issn1002-0306.2021080184 |
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| author | Xiangju ZHOU Yuqin CHEN Zhongping YIN Qi LIANG ZANG Jianwei Daobang TANG Jiguang CHEN |
| author_facet | Xiangju ZHOU Yuqin CHEN Zhongping YIN Qi LIANG ZANG Jianwei Daobang TANG Jiguang CHEN |
| author_sort | Xiangju ZHOU |
| collection | DOAJ |
| description | To investigate the inhibitory activity and mechanism of naringin on α-glucosidase, the inhibition effect, type, and molecular mechanism of naringin on α-glucosidase were investigated by integrative analysis of enzyme kinetics, fluorescence spectroscopy and molecular docking simulation. The results showed that IC50 of naringin against α-glucosidase was 0.174 mmol/L, which was significantly lower than that of acarbose (IC50=0.721 mmol/L). The inhibition type was non-competitive inhibition with a Ki of 0.114 mmol/L. The binding of naringin and α-glucosidase led to the internal fluorescence quenching of the enzyme molecule. Furhter analysis indicated that the quenching constant was 0.1598×104 L/mol, and there was only one binding site. The molecular docking results showed that naringin was bound to a hydrophobic pocket of α-glucoside enzyme by the driving force of hydrogen bond, ionic bond, hydrophobic action, π-π-T stacking, and electrostatic action, with a binding energy of −7.6 kJ/mol. The results indicated that naringin was a good food-borne α-glucosidase inhibitor, and therefore had a good application prospect in the adjuvant treatment of diabetes functional food. |
| first_indexed | 2024-04-11T06:52:33Z |
| format | Article |
| id | doaj.art-89646036b14b411d9a913f5b8e1492e4 |
| institution | Directory Open Access Journal |
| issn | 1002-0306 |
| language | zho |
| last_indexed | 2024-04-11T06:52:33Z |
| publishDate | 2022-04-01 |
| publisher | The editorial department of Science and Technology of Food Industry |
| record_format | Article |
| series | Shipin gongye ke-ji |
| spelling | doaj.art-89646036b14b411d9a913f5b8e1492e42022-12-22T04:39:08ZzhoThe editorial department of Science and Technology of Food IndustryShipin gongye ke-ji1002-03062022-04-0143815716410.13386/j.issn1002-0306.20210801842021080184-8Inhibitory Effect of Naringin on α-Glucosidase and Its MechanismXiangju ZHOU0Yuqin CHEN1Zhongping YIN2Qi LIANG3ZANG Jianwei4Daobang TANG5Jiguang CHEN6College of Food Science and Engineering, Jiangxi Key Laboratory of Natural Products and Functional Foods/Jiangxi Engineering Laboratory of Agricultural Products Processing and Safety Control, Jiangxi Agricultural University, Nanchang 330045, ChinaCollege of Food Science and Engineering, Jiangxi Key Laboratory of Natural Products and Functional Foods/Jiangxi Engineering Laboratory of Agricultural Products Processing and Safety Control, Jiangxi Agricultural University, Nanchang 330045, ChinaCollege of Food Science and Engineering, Jiangxi Key Laboratory of Natural Products and Functional Foods/Jiangxi Engineering Laboratory of Agricultural Products Processing and Safety Control, Jiangxi Agricultural University, Nanchang 330045, ChinaCollege of Food Science and Engineering, Jiangxi Key Laboratory of Natural Products and Functional Foods/Jiangxi Engineering Laboratory of Agricultural Products Processing and Safety Control, Jiangxi Agricultural University, Nanchang 330045, ChinaCollege of Food Science and Engineering, Jiangxi Key Laboratory of Natural Products and Functional Foods/Jiangxi Engineering Laboratory of Agricultural Products Processing and Safety Control, Jiangxi Agricultural University, Nanchang 330045, ChinaInstitute of Sericulture and Agro-Products Processing, Guangdong Academy of Agricultural Sciences, Guangdong Key Laboratory of Agro-Products Processing/Key Laboratory of Functional Food, Guangzhou 510610, ChinaCollege of Food Science and Engineering, Jiangxi Key Laboratory of Natural Products and Functional Foods/Jiangxi Engineering Laboratory of Agricultural Products Processing and Safety Control, Jiangxi Agricultural University, Nanchang 330045, ChinaTo investigate the inhibitory activity and mechanism of naringin on α-glucosidase, the inhibition effect, type, and molecular mechanism of naringin on α-glucosidase were investigated by integrative analysis of enzyme kinetics, fluorescence spectroscopy and molecular docking simulation. The results showed that IC50 of naringin against α-glucosidase was 0.174 mmol/L, which was significantly lower than that of acarbose (IC50=0.721 mmol/L). The inhibition type was non-competitive inhibition with a Ki of 0.114 mmol/L. The binding of naringin and α-glucosidase led to the internal fluorescence quenching of the enzyme molecule. Furhter analysis indicated that the quenching constant was 0.1598×104 L/mol, and there was only one binding site. The molecular docking results showed that naringin was bound to a hydrophobic pocket of α-glucoside enzyme by the driving force of hydrogen bond, ionic bond, hydrophobic action, π-π-T stacking, and electrostatic action, with a binding energy of −7.6 kJ/mol. The results indicated that naringin was a good food-borne α-glucosidase inhibitor, and therefore had a good application prospect in the adjuvant treatment of diabetes functional food.http://www.spgykj.com/cn/article/doi/10.13386/j.issn1002-0306.2021080184naringeninα-glucosidasefluorescence spectroscopymolecular dockinginhibition |
| spellingShingle | Xiangju ZHOU Yuqin CHEN Zhongping YIN Qi LIANG ZANG Jianwei Daobang TANG Jiguang CHEN Inhibitory Effect of Naringin on α-Glucosidase and Its Mechanism Shipin gongye ke-ji naringenin α-glucosidase fluorescence spectroscopy molecular docking inhibition |
| title | Inhibitory Effect of Naringin on α-Glucosidase and Its Mechanism |
| title_full | Inhibitory Effect of Naringin on α-Glucosidase and Its Mechanism |
| title_fullStr | Inhibitory Effect of Naringin on α-Glucosidase and Its Mechanism |
| title_full_unstemmed | Inhibitory Effect of Naringin on α-Glucosidase and Its Mechanism |
| title_short | Inhibitory Effect of Naringin on α-Glucosidase and Its Mechanism |
| title_sort | inhibitory effect of naringin on α glucosidase and its mechanism |
| topic | naringenin α-glucosidase fluorescence spectroscopy molecular docking inhibition |
| url | http://www.spgykj.com/cn/article/doi/10.13386/j.issn1002-0306.2021080184 |
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