Condensed Tannins from Longan Bark as Inhibitor of Tyrosinase: Structure, Activity, and Mechanism
In this study, the content, structure, antityrosinase activity, and mechanism of longan bark condensed tannins were evaluated. The findings obtained from mass spectrometry demonstrated that longan bark condensed tannins were mixtures of procyanidins, propelargonidins, prodelphinidins, and their acyl...
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| Veröffentlicht in: | Journal of agricultural and food chemistry 2018-01, Vol.66 (4), p.908-917 |
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| container_title | Journal of agricultural and food chemistry |
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| creator | Chai, Wei-Ming Huang, Qian Lin, Mei-Zhen Ou-Yang, Chong Huang, Wen-Yang Wang, Ying-Xia Xu, Kai-Li Feng, Hui-Ling |
| description | In this study, the content, structure, antityrosinase activity, and mechanism of longan bark condensed tannins were evaluated. The findings obtained from mass spectrometry demonstrated that longan bark condensed tannins were mixtures of procyanidins, propelargonidins, prodelphinidins, and their acyl derivatives (galloyl and p-hydroxybenzoate). The enzyme analysis indicated that these mixtures were efficient, reversible, and mixed (competitive is dominant) inhibitor of tyrosinase. What’s more, the mixtures showed good inhibitions on proliferation, intracellular enzyme activity and melanogenesis of mouse melanoma cells (B16). From molecular docking, the results showed the interactions between inhibitors and tyrosinase were driven by hydrogen bond, electrostatic, and hydrophobic interactions. In addition, high levels of total phenolic and extractable condensed tannins suggested that longan bark might be a good source of tyrosinase inhibitor. This study would offer theoretical basis for the development of longan bark condensed tannins as novel food preservatives and medicines of skin diseases. |
| doi_str_mv | 10.1021/acs.jafc.7b05481 |
| format | Article |
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The findings obtained from mass spectrometry demonstrated that longan bark condensed tannins were mixtures of procyanidins, propelargonidins, prodelphinidins, and their acyl derivatives (galloyl and p-hydroxybenzoate). The enzyme analysis indicated that these mixtures were efficient, reversible, and mixed (competitive is dominant) inhibitor of tyrosinase. What’s more, the mixtures showed good inhibitions on proliferation, intracellular enzyme activity and melanogenesis of mouse melanoma cells (B16). From molecular docking, the results showed the interactions between inhibitors and tyrosinase were driven by hydrogen bond, electrostatic, and hydrophobic interactions. In addition, high levels of total phenolic and extractable condensed tannins suggested that longan bark might be a good source of tyrosinase inhibitor. This study would offer theoretical basis for the development of longan bark condensed tannins as novel food preservatives and medicines of skin diseases.</description><identifier>ISSN: 0021-8561</identifier><identifier>EISSN: 1520-5118</identifier><identifier>DOI: 10.1021/acs.jafc.7b05481</identifier><identifier>PMID: 29313327</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Animals ; Anthocyanins - pharmacology ; Biflavonoids - pharmacology ; Catechin - pharmacology ; Cell Proliferation - drug effects ; Enzyme Inhibitors - pharmacology ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Mass Spectrometry ; Melanins - analysis ; Melanins - antagonists & inhibitors ; Melanins - biosynthesis ; Melanoma, Experimental ; Mice ; Models, Molecular ; Molecular Docking Simulation ; Monophenol Monooxygenase - antagonists & inhibitors ; Oxidoreductases ; Parabens - pharmacology ; Plant Bark - chemistry ; Proanthocyanidins - pharmacology ; Sapindaceae - chemistry ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Static Electricity ; Structure-Activity Relationship ; Tannins - chemistry ; Tannins - pharmacology</subject><ispartof>Journal of agricultural and food chemistry, 2018-01, Vol.66 (4), p.908-917</ispartof><rights>Copyright © 2018 American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a336t-f803ca624af2188e917d99914d1837e88d17c0bfb894cbb404c95aa4f36ac2073</citedby><cites>FETCH-LOGICAL-a336t-f803ca624af2188e917d99914d1837e88d17c0bfb894cbb404c95aa4f36ac2073</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/acs.jafc.7b05481$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/acs.jafc.7b05481$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,777,781,2752,27057,27905,27906,56719,56769</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29313327$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Chai, Wei-Ming</creatorcontrib><creatorcontrib>Huang, Qian</creatorcontrib><creatorcontrib>Lin, Mei-Zhen</creatorcontrib><creatorcontrib>Ou-Yang, Chong</creatorcontrib><creatorcontrib>Huang, Wen-Yang</creatorcontrib><creatorcontrib>Wang, Ying-Xia</creatorcontrib><creatorcontrib>Xu, Kai-Li</creatorcontrib><creatorcontrib>Feng, Hui-Ling</creatorcontrib><title>Condensed Tannins from Longan Bark as Inhibitor of Tyrosinase: Structure, Activity, and Mechanism</title><title>Journal of agricultural and food chemistry</title><addtitle>J. Agric. Food Chem</addtitle><description>In this study, the content, structure, antityrosinase activity, and mechanism of longan bark condensed tannins were evaluated. The findings obtained from mass spectrometry demonstrated that longan bark condensed tannins were mixtures of procyanidins, propelargonidins, prodelphinidins, and their acyl derivatives (galloyl and p-hydroxybenzoate). The enzyme analysis indicated that these mixtures were efficient, reversible, and mixed (competitive is dominant) inhibitor of tyrosinase. What’s more, the mixtures showed good inhibitions on proliferation, intracellular enzyme activity and melanogenesis of mouse melanoma cells (B16). From molecular docking, the results showed the interactions between inhibitors and tyrosinase were driven by hydrogen bond, electrostatic, and hydrophobic interactions. In addition, high levels of total phenolic and extractable condensed tannins suggested that longan bark might be a good source of tyrosinase inhibitor. This study would offer theoretical basis for the development of longan bark condensed tannins as novel food preservatives and medicines of skin diseases.</description><subject>Animals</subject><subject>Anthocyanins - pharmacology</subject><subject>Biflavonoids - pharmacology</subject><subject>Catechin - pharmacology</subject><subject>Cell Proliferation - drug effects</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Hydrogen Bonding</subject><subject>Hydrophobic and Hydrophilic Interactions</subject><subject>Mass Spectrometry</subject><subject>Melanins - analysis</subject><subject>Melanins - antagonists & inhibitors</subject><subject>Melanins - biosynthesis</subject><subject>Melanoma, Experimental</subject><subject>Mice</subject><subject>Models, Molecular</subject><subject>Molecular Docking Simulation</subject><subject>Monophenol Monooxygenase - antagonists & inhibitors</subject><subject>Oxidoreductases</subject><subject>Parabens - pharmacology</subject><subject>Plant Bark - chemistry</subject><subject>Proanthocyanidins - pharmacology</subject><subject>Sapindaceae - chemistry</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><subject>Static Electricity</subject><subject>Structure-Activity Relationship</subject><subject>Tannins - chemistry</subject><subject>Tannins - pharmacology</subject><issn>0021-8561</issn><issn>1520-5118</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kD1PwzAURS0EglLYmZBHhqb4xUljs0HFR6UiBsocvTg2NTQ22AlS_z0pLWxMdzn3SvcQcgZsDCyFS1Rx_IZGjYuK5ZmAPTKAPGVJDiD2yYD1TCLyCRyR4xjfGGMiL9ghOUolB87TYkBw6l2tXdQ1XaBz1kVqgm_o3LtXdPQGwzvFSGduaSvb-kC9oYt18NE6jPqKPrehU20X9Iheq9Z-2XY9ouhq-qjVEp2NzQk5MLiK-nSXQ_Jyd7uYPiTzp_vZ9HqeIOeTNjGCcYWTNEOTghBaQlFLKSGrQfBCC1FDoVhlKiEzVVUZy5TMETPDJ6hSVvAhudjufgT_2enYlo2NSq9W6LTvYglSyLwAyHmPsi2q-iMxaFN-BNtgWJfAyo3YshdbbsSWO7F95Xy33lWNrv8KvyZ7YLQFfqq-C64_-__eN3ffhBI</recordid><startdate>20180131</startdate><enddate>20180131</enddate><creator>Chai, Wei-Ming</creator><creator>Huang, Qian</creator><creator>Lin, Mei-Zhen</creator><creator>Ou-Yang, Chong</creator><creator>Huang, Wen-Yang</creator><creator>Wang, Ying-Xia</creator><creator>Xu, Kai-Li</creator><creator>Feng, Hui-Ling</creator><general>American Chemical Society</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20180131</creationdate><title>Condensed Tannins from Longan Bark as Inhibitor of Tyrosinase: Structure, Activity, and Mechanism</title><author>Chai, Wei-Ming ; Huang, Qian ; Lin, Mei-Zhen ; Ou-Yang, Chong ; Huang, Wen-Yang ; Wang, Ying-Xia ; Xu, Kai-Li ; Feng, Hui-Ling</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a336t-f803ca624af2188e917d99914d1837e88d17c0bfb894cbb404c95aa4f36ac2073</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Animals</topic><topic>Anthocyanins - pharmacology</topic><topic>Biflavonoids - pharmacology</topic><topic>Catechin - pharmacology</topic><topic>Cell Proliferation - drug effects</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Hydrogen Bonding</topic><topic>Hydrophobic and Hydrophilic Interactions</topic><topic>Mass Spectrometry</topic><topic>Melanins - analysis</topic><topic>Melanins - antagonists & inhibitors</topic><topic>Melanins - biosynthesis</topic><topic>Melanoma, Experimental</topic><topic>Mice</topic><topic>Models, Molecular</topic><topic>Molecular Docking Simulation</topic><topic>Monophenol Monooxygenase - antagonists & inhibitors</topic><topic>Oxidoreductases</topic><topic>Parabens - pharmacology</topic><topic>Plant Bark - chemistry</topic><topic>Proanthocyanidins - pharmacology</topic><topic>Sapindaceae - chemistry</topic><topic>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</topic><topic>Static Electricity</topic><topic>Structure-Activity Relationship</topic><topic>Tannins - chemistry</topic><topic>Tannins - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chai, Wei-Ming</creatorcontrib><creatorcontrib>Huang, Qian</creatorcontrib><creatorcontrib>Lin, Mei-Zhen</creatorcontrib><creatorcontrib>Ou-Yang, Chong</creatorcontrib><creatorcontrib>Huang, Wen-Yang</creatorcontrib><creatorcontrib>Wang, Ying-Xia</creatorcontrib><creatorcontrib>Xu, Kai-Li</creatorcontrib><creatorcontrib>Feng, Hui-Ling</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of agricultural and food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chai, Wei-Ming</au><au>Huang, Qian</au><au>Lin, Mei-Zhen</au><au>Ou-Yang, Chong</au><au>Huang, Wen-Yang</au><au>Wang, Ying-Xia</au><au>Xu, Kai-Li</au><au>Feng, Hui-Ling</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Condensed Tannins from Longan Bark as Inhibitor of Tyrosinase: Structure, Activity, and Mechanism</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>2018-01-31</date><risdate>2018</risdate><volume>66</volume><issue>4</issue><spage>908</spage><epage>917</epage><pages>908-917</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><abstract>In this study, the content, structure, antityrosinase activity, and mechanism of longan bark condensed tannins were evaluated. The findings obtained from mass spectrometry demonstrated that longan bark condensed tannins were mixtures of procyanidins, propelargonidins, prodelphinidins, and their acyl derivatives (galloyl and p-hydroxybenzoate). The enzyme analysis indicated that these mixtures were efficient, reversible, and mixed (competitive is dominant) inhibitor of tyrosinase. What’s more, the mixtures showed good inhibitions on proliferation, intracellular enzyme activity and melanogenesis of mouse melanoma cells (B16). From molecular docking, the results showed the interactions between inhibitors and tyrosinase were driven by hydrogen bond, electrostatic, and hydrophobic interactions. In addition, high levels of total phenolic and extractable condensed tannins suggested that longan bark might be a good source of tyrosinase inhibitor. This study would offer theoretical basis for the development of longan bark condensed tannins as novel food preservatives and medicines of skin diseases.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>29313327</pmid><doi>10.1021/acs.jafc.7b05481</doi><tpages>10</tpages></addata></record> |
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| subjects | Animals Anthocyanins - pharmacology Biflavonoids - pharmacology Catechin - pharmacology Cell Proliferation - drug effects Enzyme Inhibitors - pharmacology Hydrogen Bonding Hydrophobic and Hydrophilic Interactions Mass Spectrometry Melanins - analysis Melanins - antagonists & inhibitors Melanins - biosynthesis Melanoma, Experimental Mice Models, Molecular Molecular Docking Simulation Monophenol Monooxygenase - antagonists & inhibitors Oxidoreductases Parabens - pharmacology Plant Bark - chemistry Proanthocyanidins - pharmacology Sapindaceae - chemistry Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Static Electricity Structure-Activity Relationship Tannins - chemistry Tannins - pharmacology |
| title | Condensed Tannins from Longan Bark as Inhibitor of Tyrosinase: Structure, Activity, and Mechanism |
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