Inhibitory effects of phenolic glycosides from Bunge on α-glucosidase: inhibition kinetics and mechanisms
Two undescribed phenolic glycosides, trochinenols B and C ( 1 and 2 ), together with four known analogues ( 3-6 ), were isolated from the functional tea Trollius chinensis Bunge and their α-glucosidase inhibitory kinetics and mechanisms were investigated. It was found that 1 inhibited α-glucosidase...
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| Veröffentlicht in: | Food & function 2022-03, Vol.13 (5), p.2857-2864 |
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| creator | Feng, Jie He, Fengming Huang, Yuhui Zhou, Mi Liu, Xiangzhong Ye, Xiansheng Yang, Renjing Tian, Wenjing Chen, Haifeng |
| description | Two undescribed phenolic glycosides, trochinenols B and C (
1 and
2
), together with four known analogues (
3-6
), were isolated from the functional tea
Trollius chinensis
Bunge and their α-glucosidase inhibitory kinetics and mechanisms were investigated. It was found that
1
inhibited α-glucosidase in a noncompetitive manner with an IC
50
value of 25.96 μM, while
3
showed a notable inhibitory effect against α-glucosidase in an uncompetitive manner with an IC
50
value of 3.14 μM. Analysis of synchronous fluorescence and circular dichroism spectroscopy indicated that the binding of
1
to α-glucosidase led to the rearrangement and conformational alteration of the α-glucosidase enzyme. Furthermore, molecular docking indicated that
1
had a high affinity close to the active site pocket of α-glucosidase and indirectly inhibited the catalytic activity of the enzyme. However,
3
was bound to the entrance part of the active center of α-glucosidase and could hinder the release of the substrate as well as the catalytic reaction product, eventually suppressing the catalytic activity of α-glucosidase.
Inhibitory effects of phenolic glycosides from the functional tea
Trollius chinensis
Bunge on α-glucosidase: inhibition kinetics and mechanisms. |
| doi_str_mv | 10.1039/d1fo03347f |
| format | Article |
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1 and
2
), together with four known analogues (
3-6
), were isolated from the functional tea
Trollius chinensis
Bunge and their α-glucosidase inhibitory kinetics and mechanisms were investigated. It was found that
1
inhibited α-glucosidase in a noncompetitive manner with an IC
50
value of 25.96 μM, while
3
showed a notable inhibitory effect against α-glucosidase in an uncompetitive manner with an IC
50
value of 3.14 μM. Analysis of synchronous fluorescence and circular dichroism spectroscopy indicated that the binding of
1
to α-glucosidase led to the rearrangement and conformational alteration of the α-glucosidase enzyme. Furthermore, molecular docking indicated that
1
had a high affinity close to the active site pocket of α-glucosidase and indirectly inhibited the catalytic activity of the enzyme. However,
3
was bound to the entrance part of the active center of α-glucosidase and could hinder the release of the substrate as well as the catalytic reaction product, eventually suppressing the catalytic activity of α-glucosidase.
Inhibitory effects of phenolic glycosides from the functional tea
Trollius chinensis
Bunge on α-glucosidase: inhibition kinetics and mechanisms.</description><identifier>ISSN: 2042-6496</identifier><identifier>EISSN: 2042-650X</identifier><identifier>DOI: 10.1039/d1fo03347f</identifier><ispartof>Food & function, 2022-03, Vol.13 (5), p.2857-2864</ispartof><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids></links><search><creatorcontrib>Feng, Jie</creatorcontrib><creatorcontrib>He, Fengming</creatorcontrib><creatorcontrib>Huang, Yuhui</creatorcontrib><creatorcontrib>Zhou, Mi</creatorcontrib><creatorcontrib>Liu, Xiangzhong</creatorcontrib><creatorcontrib>Ye, Xiansheng</creatorcontrib><creatorcontrib>Yang, Renjing</creatorcontrib><creatorcontrib>Tian, Wenjing</creatorcontrib><creatorcontrib>Chen, Haifeng</creatorcontrib><title>Inhibitory effects of phenolic glycosides from Bunge on α-glucosidase: inhibition kinetics and mechanisms</title><title>Food & function</title><description>Two undescribed phenolic glycosides, trochinenols B and C (
1 and
2
), together with four known analogues (
3-6
), were isolated from the functional tea
Trollius chinensis
Bunge and their α-glucosidase inhibitory kinetics and mechanisms were investigated. It was found that
1
inhibited α-glucosidase in a noncompetitive manner with an IC
50
value of 25.96 μM, while
3
showed a notable inhibitory effect against α-glucosidase in an uncompetitive manner with an IC
50
value of 3.14 μM. Analysis of synchronous fluorescence and circular dichroism spectroscopy indicated that the binding of
1
to α-glucosidase led to the rearrangement and conformational alteration of the α-glucosidase enzyme. Furthermore, molecular docking indicated that
1
had a high affinity close to the active site pocket of α-glucosidase and indirectly inhibited the catalytic activity of the enzyme. However,
3
was bound to the entrance part of the active center of α-glucosidase and could hinder the release of the substrate as well as the catalytic reaction product, eventually suppressing the catalytic activity of α-glucosidase.
Inhibitory effects of phenolic glycosides from the functional tea
Trollius chinensis
Bunge on α-glucosidase: inhibition kinetics and mechanisms.</description><issn>2042-6496</issn><issn>2042-650X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid/><recordid>eNqFj71uwjAUhS1UJFBhYUe6LxDq4PBjRhCo3RnYkHGukwuJjXzDkMfiRfpMRbRVx57lO9InHekIMUrlJJVKv-WpC1KpbOE6oj-V2TSZz-Th5bdnet4TQ-azfERpvdTLvjh_-JJO1ITYAjqHtmEIDq4l-lCRhaJqbWDKkcHFUMP65guE4OHznhTV7ekM4wroe4ce6kIeG7IMxudQoy2NJ655ILrOVIzDH76K8W6737wnke3xGqk2sT3-fVD_-S8lhkyx</recordid><startdate>20220307</startdate><enddate>20220307</enddate><creator>Feng, Jie</creator><creator>He, Fengming</creator><creator>Huang, Yuhui</creator><creator>Zhou, Mi</creator><creator>Liu, Xiangzhong</creator><creator>Ye, Xiansheng</creator><creator>Yang, Renjing</creator><creator>Tian, Wenjing</creator><creator>Chen, Haifeng</creator><scope/></search><sort><creationdate>20220307</creationdate><title>Inhibitory effects of phenolic glycosides from Bunge on α-glucosidase: inhibition kinetics and mechanisms</title><author>Feng, Jie ; He, Fengming ; Huang, Yuhui ; Zhou, Mi ; Liu, Xiangzhong ; Ye, Xiansheng ; Yang, Renjing ; Tian, Wenjing ; Chen, Haifeng</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-rsc_primary_d1fo03347f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><creationdate>2022</creationdate><toplevel>online_resources</toplevel><creatorcontrib>Feng, Jie</creatorcontrib><creatorcontrib>He, Fengming</creatorcontrib><creatorcontrib>Huang, Yuhui</creatorcontrib><creatorcontrib>Zhou, Mi</creatorcontrib><creatorcontrib>Liu, Xiangzhong</creatorcontrib><creatorcontrib>Ye, Xiansheng</creatorcontrib><creatorcontrib>Yang, Renjing</creatorcontrib><creatorcontrib>Tian, Wenjing</creatorcontrib><creatorcontrib>Chen, Haifeng</creatorcontrib><jtitle>Food & function</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Feng, Jie</au><au>He, Fengming</au><au>Huang, Yuhui</au><au>Zhou, Mi</au><au>Liu, Xiangzhong</au><au>Ye, Xiansheng</au><au>Yang, Renjing</au><au>Tian, Wenjing</au><au>Chen, Haifeng</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Inhibitory effects of phenolic glycosides from Bunge on α-glucosidase: inhibition kinetics and mechanisms</atitle><jtitle>Food & function</jtitle><date>2022-03-07</date><risdate>2022</risdate><volume>13</volume><issue>5</issue><spage>2857</spage><epage>2864</epage><pages>2857-2864</pages><issn>2042-6496</issn><eissn>2042-650X</eissn><abstract>Two undescribed phenolic glycosides, trochinenols B and C (
1 and
2
), together with four known analogues (
3-6
), were isolated from the functional tea
Trollius chinensis
Bunge and their α-glucosidase inhibitory kinetics and mechanisms were investigated. It was found that
1
inhibited α-glucosidase in a noncompetitive manner with an IC
50
value of 25.96 μM, while
3
showed a notable inhibitory effect against α-glucosidase in an uncompetitive manner with an IC
50
value of 3.14 μM. Analysis of synchronous fluorescence and circular dichroism spectroscopy indicated that the binding of
1
to α-glucosidase led to the rearrangement and conformational alteration of the α-glucosidase enzyme. Furthermore, molecular docking indicated that
1
had a high affinity close to the active site pocket of α-glucosidase and indirectly inhibited the catalytic activity of the enzyme. However,
3
was bound to the entrance part of the active center of α-glucosidase and could hinder the release of the substrate as well as the catalytic reaction product, eventually suppressing the catalytic activity of α-glucosidase.
Inhibitory effects of phenolic glycosides from the functional tea
Trollius chinensis
Bunge on α-glucosidase: inhibition kinetics and mechanisms.</abstract><doi>10.1039/d1fo03347f</doi><tpages>8</tpages></addata></record> |
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| source | Royal Society Of Chemistry Journals 2008- |
| title | Inhibitory effects of phenolic glycosides from Bunge on α-glucosidase: inhibition kinetics and mechanisms |
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