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Synthesis and biological evaluation of coumarin derivatives as α-glucosidase inhibitors
In this study, two series of coumarin derivatives 5a∼i and 6a∼i were synthesized, and their inhibitory activity against α-glucosidase was determined. The results indicated that most of the synthesized derivatives exhibited prominent inhibitory activities against α-glucosidase. Among them, compounds...
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| Published in: | European journal of medicinal chemistry 2020-03, Vol.189, p.112013-112013, Article 112013 |
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| Main Authors: | , , , , , , , , , , , , |
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| cites | cdi_FETCH-LOGICAL-c362t-f1690f53e5aa9c8c0a7e0d492532bdf59d316b5c3e9ad7ad8e0539e2c6053c523 |
| container_end_page | 112013 |
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| container_title | European journal of medicinal chemistry |
| container_volume | 189 |
| creator | Xu, Xue-Tao Deng, Xu-Yang Chen, Jie Liang, Qi-Ming Zhang, Kun Li, Dong-Li Wu, Pan-Pan Zheng, Xi Zhou, Ren-Ping Jiang, Zheng-Yun Ma, Ai-Jun Chen, Wen-Hua Wang, Shao-Hua |
| description | In this study, two series of coumarin derivatives 5a∼i and 6a∼i were synthesized, and their inhibitory activity against α-glucosidase was determined. The results indicated that most of the synthesized derivatives exhibited prominent inhibitory activities against α-glucosidase. Among them, compounds 5a and 5b showed the strongest inhibition with the IC50 values of 19.64 μM and 12.98 μM, respectively. Enzyme kinetic studies of compounds 5a and 5b proved that their inhibition was reversible and a mixed type. The KI and KIS values of compound 5a were calculated to be 27.39 μM and 13.02 μM, respectively, and the corresponding values for compound 5b being 27.02 μM and 13.65 μM, respectively. The docking studies showed that compound 5b could be inserted into the active pocket of α-glucosidase and form hydrogen bonds with LYS293 to enhance the binding affinity.
[Display omitted]
•Coumarin derivatives 5 (a ∼ i) and 6 (a ∼ i) were synthesized.•The synthetic compounds were screened for α-glucosidase inhibitory activity.•Kinetic studies determined the mechanism of synthetic compounds on α-glucosidase.•In silico studies were performed to confirm the binding interactions of synthetic compounds with the enzyme active site. |
| doi_str_mv | 10.1016/j.ejmech.2019.112013 |
| format | article |
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[Display omitted]
•Coumarin derivatives 5 (a ∼ i) and 6 (a ∼ i) were synthesized.•The synthetic compounds were screened for α-glucosidase inhibitory activity.•Kinetic studies determined the mechanism of synthetic compounds on α-glucosidase.•In silico studies were performed to confirm the binding interactions of synthetic compounds with the enzyme active site.</description><identifier>ISSN: 0223-5234</identifier><identifier>EISSN: 1768-3254</identifier><identifier>DOI: 10.1016/j.ejmech.2019.112013</identifier><identifier>PMID: 31972390</identifier><language>eng</language><publisher>France: Elsevier Masson SAS</publisher><subject>Cinnamic acid ; Coumarin ; Enzyme inhibition ; Molecular docking ; Synthesis ; α-Glucosidase</subject><ispartof>European journal of medicinal chemistry, 2020-03, Vol.189, p.112013-112013, Article 112013</ispartof><rights>2019</rights><rights>Copyright © 2019. Published by Elsevier Masson SAS.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c362t-f1690f53e5aa9c8c0a7e0d492532bdf59d316b5c3e9ad7ad8e0539e2c6053c523</citedby><cites>FETCH-LOGICAL-c362t-f1690f53e5aa9c8c0a7e0d492532bdf59d316b5c3e9ad7ad8e0539e2c6053c523</cites><orcidid>0000-0002-6515-0726 ; 0000-0002-6919-948X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,786,790,27957,27958</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31972390$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Xu, Xue-Tao</creatorcontrib><creatorcontrib>Deng, Xu-Yang</creatorcontrib><creatorcontrib>Chen, Jie</creatorcontrib><creatorcontrib>Liang, Qi-Ming</creatorcontrib><creatorcontrib>Zhang, Kun</creatorcontrib><creatorcontrib>Li, Dong-Li</creatorcontrib><creatorcontrib>Wu, Pan-Pan</creatorcontrib><creatorcontrib>Zheng, Xi</creatorcontrib><creatorcontrib>Zhou, Ren-Ping</creatorcontrib><creatorcontrib>Jiang, Zheng-Yun</creatorcontrib><creatorcontrib>Ma, Ai-Jun</creatorcontrib><creatorcontrib>Chen, Wen-Hua</creatorcontrib><creatorcontrib>Wang, Shao-Hua</creatorcontrib><title>Synthesis and biological evaluation of coumarin derivatives as α-glucosidase inhibitors</title><title>European journal of medicinal chemistry</title><addtitle>Eur J Med Chem</addtitle><description>In this study, two series of coumarin derivatives 5a∼i and 6a∼i were synthesized, and their inhibitory activity against α-glucosidase was determined. The results indicated that most of the synthesized derivatives exhibited prominent inhibitory activities against α-glucosidase. Among them, compounds 5a and 5b showed the strongest inhibition with the IC50 values of 19.64 μM and 12.98 μM, respectively. Enzyme kinetic studies of compounds 5a and 5b proved that their inhibition was reversible and a mixed type. The KI and KIS values of compound 5a were calculated to be 27.39 μM and 13.02 μM, respectively, and the corresponding values for compound 5b being 27.02 μM and 13.65 μM, respectively. The docking studies showed that compound 5b could be inserted into the active pocket of α-glucosidase and form hydrogen bonds with LYS293 to enhance the binding affinity.
[Display omitted]
•Coumarin derivatives 5 (a ∼ i) and 6 (a ∼ i) were synthesized.•The synthetic compounds were screened for α-glucosidase inhibitory activity.•Kinetic studies determined the mechanism of synthetic compounds on α-glucosidase.•In silico studies were performed to confirm the binding interactions of synthetic compounds with the enzyme active site.</description><subject>Cinnamic acid</subject><subject>Coumarin</subject><subject>Enzyme inhibition</subject><subject>Molecular docking</subject><subject>Synthesis</subject><subject>α-Glucosidase</subject><issn>0223-5234</issn><issn>1768-3254</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><recordid>eNp9kM1KAzEUhYMotlbfQGSWbqbmZzLTbAQp_kHBhQruQia506ZMJzWZGehj-SI-kylTXbo6cDnnHs6H0CXBU4JJfrOewnoDejWlmIgpIVHYERqTIp-ljPLsGI0xpSzllGUjdBbCGmPMc4xP0YgRUVAm8Bh9vO6adgXBhkQ1Jimtq93SalUn0Ku6U611TeKqRLtuo7xtEgPe9vHcQ0yE5PsrXdaddsEaFSCxzcqWtnU-nKOTStUBLg46Qe8P92_zp3Tx8vg8v1ukmuW0TSuSC1xxBlwpoWcaqwKwyQTljJam4sIwkpdcMxDKFMrMAHMmgOo8qo7bJuh6-Lv17rOD0MqNDRrqWjXguiDj-owWlHMcrdlg1d6F4KGSW2_jqp0kWO6ZyrUcmMo9UzkwjbGrQ0NXbsD8hX4hRsPtYIC4s7fgZdAWGg3GetCtNM7-3_ADLrqLVw</recordid><startdate>20200301</startdate><enddate>20200301</enddate><creator>Xu, Xue-Tao</creator><creator>Deng, Xu-Yang</creator><creator>Chen, Jie</creator><creator>Liang, Qi-Ming</creator><creator>Zhang, Kun</creator><creator>Li, Dong-Li</creator><creator>Wu, Pan-Pan</creator><creator>Zheng, Xi</creator><creator>Zhou, Ren-Ping</creator><creator>Jiang, Zheng-Yun</creator><creator>Ma, Ai-Jun</creator><creator>Chen, Wen-Hua</creator><creator>Wang, Shao-Hua</creator><general>Elsevier Masson SAS</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-6515-0726</orcidid><orcidid>https://orcid.org/0000-0002-6919-948X</orcidid></search><sort><creationdate>20200301</creationdate><title>Synthesis and biological evaluation of coumarin derivatives as α-glucosidase inhibitors</title><author>Xu, Xue-Tao ; Deng, Xu-Yang ; Chen, Jie ; Liang, Qi-Ming ; Zhang, Kun ; Li, Dong-Li ; Wu, Pan-Pan ; Zheng, Xi ; Zhou, Ren-Ping ; Jiang, Zheng-Yun ; Ma, Ai-Jun ; Chen, Wen-Hua ; Wang, Shao-Hua</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c362t-f1690f53e5aa9c8c0a7e0d492532bdf59d316b5c3e9ad7ad8e0539e2c6053c523</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Cinnamic acid</topic><topic>Coumarin</topic><topic>Enzyme inhibition</topic><topic>Molecular docking</topic><topic>Synthesis</topic><topic>α-Glucosidase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Xu, Xue-Tao</creatorcontrib><creatorcontrib>Deng, Xu-Yang</creatorcontrib><creatorcontrib>Chen, Jie</creatorcontrib><creatorcontrib>Liang, Qi-Ming</creatorcontrib><creatorcontrib>Zhang, Kun</creatorcontrib><creatorcontrib>Li, Dong-Li</creatorcontrib><creatorcontrib>Wu, Pan-Pan</creatorcontrib><creatorcontrib>Zheng, Xi</creatorcontrib><creatorcontrib>Zhou, Ren-Ping</creatorcontrib><creatorcontrib>Jiang, Zheng-Yun</creatorcontrib><creatorcontrib>Ma, Ai-Jun</creatorcontrib><creatorcontrib>Chen, Wen-Hua</creatorcontrib><creatorcontrib>Wang, Shao-Hua</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>European journal of medicinal chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Xu, Xue-Tao</au><au>Deng, Xu-Yang</au><au>Chen, Jie</au><au>Liang, Qi-Ming</au><au>Zhang, Kun</au><au>Li, Dong-Li</au><au>Wu, Pan-Pan</au><au>Zheng, Xi</au><au>Zhou, Ren-Ping</au><au>Jiang, Zheng-Yun</au><au>Ma, Ai-Jun</au><au>Chen, Wen-Hua</au><au>Wang, Shao-Hua</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Synthesis and biological evaluation of coumarin derivatives as α-glucosidase inhibitors</atitle><jtitle>European journal of medicinal chemistry</jtitle><addtitle>Eur J Med Chem</addtitle><date>2020-03-01</date><risdate>2020</risdate><volume>189</volume><spage>112013</spage><epage>112013</epage><pages>112013-112013</pages><artnum>112013</artnum><issn>0223-5234</issn><eissn>1768-3254</eissn><notes>ObjectType-Article-2</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Undefined-1</notes><notes>ObjectType-Feature-3</notes><notes>content type line 23</notes><abstract>In this study, two series of coumarin derivatives 5a∼i and 6a∼i were synthesized, and their inhibitory activity against α-glucosidase was determined. The results indicated that most of the synthesized derivatives exhibited prominent inhibitory activities against α-glucosidase. Among them, compounds 5a and 5b showed the strongest inhibition with the IC50 values of 19.64 μM and 12.98 μM, respectively. Enzyme kinetic studies of compounds 5a and 5b proved that their inhibition was reversible and a mixed type. The KI and KIS values of compound 5a were calculated to be 27.39 μM and 13.02 μM, respectively, and the corresponding values for compound 5b being 27.02 μM and 13.65 μM, respectively. The docking studies showed that compound 5b could be inserted into the active pocket of α-glucosidase and form hydrogen bonds with LYS293 to enhance the binding affinity.
[Display omitted]
•Coumarin derivatives 5 (a ∼ i) and 6 (a ∼ i) were synthesized.•The synthetic compounds were screened for α-glucosidase inhibitory activity.•Kinetic studies determined the mechanism of synthetic compounds on α-glucosidase.•In silico studies were performed to confirm the binding interactions of synthetic compounds with the enzyme active site.</abstract><cop>France</cop><pub>Elsevier Masson SAS</pub><pmid>31972390</pmid><doi>10.1016/j.ejmech.2019.112013</doi><tpages>1</tpages><orcidid>https://orcid.org/0000-0002-6515-0726</orcidid><orcidid>https://orcid.org/0000-0002-6919-948X</orcidid></addata></record> |
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| language | eng |
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| source | ScienceDirect Journals |
| subjects | Cinnamic acid Coumarin Enzyme inhibition Molecular docking Synthesis α-Glucosidase |
| title | Synthesis and biological evaluation of coumarin derivatives as α-glucosidase inhibitors |
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