Rifampicin as a novel tyrosinase inhibitor: Inhibitory activity and mechanism
[Display omitted] In this study, the inhibitory effect and mechanism of rifampicin on the activity of tyrosinase were investigated for developing a novel tyrosinase inhibitor. It was found to have a significant inhibition on the activity of tyrosinase (IC50=90±0.6μM). From the kinetics analysis, it...
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| Veröffentlicht in: | International journal of biological macromolecules 2017-09, Vol.102, p.425-430 |
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| container_title | International journal of biological macromolecules |
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| creator | Chai, Wei-Ming Lin, Mei-Zhen Song, Fang-Jun Wang, Ying-Xia Xu, Kai-Li Huang, Jin-Xin Fu, Jian-Ping Peng, Yi-Yuan |
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In this study, the inhibitory effect and mechanism of rifampicin on the activity of tyrosinase were investigated for developing a novel tyrosinase inhibitor. It was found to have a significant inhibition on the activity of tyrosinase (IC50=90±0.6μM). From the kinetics analysis, it was proved to be a reversible and noncompetitive type inhibitor of the enzyme with the KI value of 94±3.5μM. The results obtained from intrinsic fluorescence quenching indicated that rifampicin could interact with tyrosinase. In particular, the drastic decrease of fluorescence intensity was due to the formation of a rifampicin-enzyme complex in a static procedure which was mainly driven by hydrophobic forces and hydrogen bonding. Moreover, the ANS-binding fluorescence analysis suggested that rifampicin binding to tyrosinase changed the polarity of the hydrophobic regions. Molecular docking analysis further revealed that the hydrogen bonds were generated between rifampicin and amino residues Leu7, Ser52, and Glu107 in the B chain of the enzyme. And the hydrophobic forces produced through the interaction of rifampicin with B chain residues Pro9, Pro14, and Trp106. This work identified a novel tyrosinase inhibitor and potentially contributed to the usage of rifampicin as a potential hyperpigmentation drug. |
| doi_str_mv | 10.1016/j.ijbiomac.2017.04.058 |
| format | Article |
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In this study, the inhibitory effect and mechanism of rifampicin on the activity of tyrosinase were investigated for developing a novel tyrosinase inhibitor. It was found to have a significant inhibition on the activity of tyrosinase (IC50=90±0.6μM). From the kinetics analysis, it was proved to be a reversible and noncompetitive type inhibitor of the enzyme with the KI value of 94±3.5μM. The results obtained from intrinsic fluorescence quenching indicated that rifampicin could interact with tyrosinase. In particular, the drastic decrease of fluorescence intensity was due to the formation of a rifampicin-enzyme complex in a static procedure which was mainly driven by hydrophobic forces and hydrogen bonding. Moreover, the ANS-binding fluorescence analysis suggested that rifampicin binding to tyrosinase changed the polarity of the hydrophobic regions. Molecular docking analysis further revealed that the hydrogen bonds were generated between rifampicin and amino residues Leu7, Ser52, and Glu107 in the B chain of the enzyme. And the hydrophobic forces produced through the interaction of rifampicin with B chain residues Pro9, Pro14, and Trp106. This work identified a novel tyrosinase inhibitor and potentially contributed to the usage of rifampicin as a potential hyperpigmentation drug.</description><identifier>ISSN: 0141-8130</identifier><identifier>EISSN: 1879-0003</identifier><identifier>DOI: 10.1016/j.ijbiomac.2017.04.058</identifier><identifier>PMID: 28414110</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Agaricales - enzymology ; Enzyme Inhibitors - metabolism ; Enzyme Inhibitors - pharmacology ; Kinetics ; Mechanism ; Molecular Docking Simulation ; Monophenol Monooxygenase - antagonists & inhibitors ; Monophenol Monooxygenase - chemistry ; Monophenol Monooxygenase - metabolism ; Protein Conformation ; Rifampicin ; Rifampin - metabolism ; Rifampin - pharmacology ; Tyrosinase inhibitor</subject><ispartof>International journal of biological macromolecules, 2017-09, Vol.102, p.425-430</ispartof><rights>2017 Elsevier B.V.</rights><rights>Copyright © 2017 Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c368t-968b4d89952de7eacf3b1f8f38d3e578575df9d3078623e0c84b0547dc20e0143</citedby><cites>FETCH-LOGICAL-c368t-968b4d89952de7eacf3b1f8f38d3e578575df9d3078623e0c84b0547dc20e0143</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.ijbiomac.2017.04.058$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28414110$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Chai, Wei-Ming</creatorcontrib><creatorcontrib>Lin, Mei-Zhen</creatorcontrib><creatorcontrib>Song, Fang-Jun</creatorcontrib><creatorcontrib>Wang, Ying-Xia</creatorcontrib><creatorcontrib>Xu, Kai-Li</creatorcontrib><creatorcontrib>Huang, Jin-Xin</creatorcontrib><creatorcontrib>Fu, Jian-Ping</creatorcontrib><creatorcontrib>Peng, Yi-Yuan</creatorcontrib><title>Rifampicin as a novel tyrosinase inhibitor: Inhibitory activity and mechanism</title><title>International journal of biological macromolecules</title><addtitle>Int J Biol Macromol</addtitle><description>[Display omitted]
In this study, the inhibitory effect and mechanism of rifampicin on the activity of tyrosinase were investigated for developing a novel tyrosinase inhibitor. It was found to have a significant inhibition on the activity of tyrosinase (IC50=90±0.6μM). From the kinetics analysis, it was proved to be a reversible and noncompetitive type inhibitor of the enzyme with the KI value of 94±3.5μM. The results obtained from intrinsic fluorescence quenching indicated that rifampicin could interact with tyrosinase. In particular, the drastic decrease of fluorescence intensity was due to the formation of a rifampicin-enzyme complex in a static procedure which was mainly driven by hydrophobic forces and hydrogen bonding. Moreover, the ANS-binding fluorescence analysis suggested that rifampicin binding to tyrosinase changed the polarity of the hydrophobic regions. Molecular docking analysis further revealed that the hydrogen bonds were generated between rifampicin and amino residues Leu7, Ser52, and Glu107 in the B chain of the enzyme. And the hydrophobic forces produced through the interaction of rifampicin with B chain residues Pro9, Pro14, and Trp106. This work identified a novel tyrosinase inhibitor and potentially contributed to the usage of rifampicin as a potential hyperpigmentation drug.</description><subject>Agaricales - enzymology</subject><subject>Enzyme Inhibitors - metabolism</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Kinetics</subject><subject>Mechanism</subject><subject>Molecular Docking Simulation</subject><subject>Monophenol Monooxygenase - antagonists & inhibitors</subject><subject>Monophenol Monooxygenase - chemistry</subject><subject>Monophenol Monooxygenase - metabolism</subject><subject>Protein Conformation</subject><subject>Rifampicin</subject><subject>Rifampin - metabolism</subject><subject>Rifampin - pharmacology</subject><subject>Tyrosinase inhibitor</subject><issn>0141-8130</issn><issn>1879-0003</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1Lw0AQhhdRbK3-hZKjl8TZbD42nhTxo1ARRM_LZndCJzRJzaaF_nu3pPXqaYaZd-blfRibc4g48OyujqguqWu0iWLgeQRJBKk8Y1Mu8yIEAHHOpsATHkouYMKunKv9NEu5vGSTWCZ-xWHK3j-p0s2GDLWBdoEO2m6H62DY952jVjsMqF1RSUPX3weLU7sPtBloR4NvWhs0aFa6Jddcs4tKrx3eHOuMfb88fz29hcuP18XT4zI0IpNDWGSyTKwsijS2mKM2lSh5JSshrcA0l2me2qqwAnKZxQLByKSENMmtiQF9KDFjt-PfTd_9bNENqiFncL3WLXZbp7iUssgyT8RLs1FqfCLXY6U2PTW63ysO6oBS1eqEUh1QKkjUeDg_emzLBu3f2YmdFzyMAvRJd4S9coawNWipRzMo29F_Hr8ssIh-</recordid><startdate>201709</startdate><enddate>201709</enddate><creator>Chai, Wei-Ming</creator><creator>Lin, Mei-Zhen</creator><creator>Song, Fang-Jun</creator><creator>Wang, Ying-Xia</creator><creator>Xu, Kai-Li</creator><creator>Huang, Jin-Xin</creator><creator>Fu, Jian-Ping</creator><creator>Peng, Yi-Yuan</creator><general>Elsevier B.V</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>201709</creationdate><title>Rifampicin as a novel tyrosinase inhibitor: Inhibitory activity and mechanism</title><author>Chai, Wei-Ming ; Lin, Mei-Zhen ; Song, Fang-Jun ; Wang, Ying-Xia ; Xu, Kai-Li ; Huang, Jin-Xin ; Fu, Jian-Ping ; Peng, Yi-Yuan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c368t-968b4d89952de7eacf3b1f8f38d3e578575df9d3078623e0c84b0547dc20e0143</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Agaricales - enzymology</topic><topic>Enzyme Inhibitors - metabolism</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Kinetics</topic><topic>Mechanism</topic><topic>Molecular Docking Simulation</topic><topic>Monophenol Monooxygenase - antagonists & inhibitors</topic><topic>Monophenol Monooxygenase - chemistry</topic><topic>Monophenol Monooxygenase - metabolism</topic><topic>Protein Conformation</topic><topic>Rifampicin</topic><topic>Rifampin - metabolism</topic><topic>Rifampin - pharmacology</topic><topic>Tyrosinase inhibitor</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chai, Wei-Ming</creatorcontrib><creatorcontrib>Lin, Mei-Zhen</creatorcontrib><creatorcontrib>Song, Fang-Jun</creatorcontrib><creatorcontrib>Wang, Ying-Xia</creatorcontrib><creatorcontrib>Xu, Kai-Li</creatorcontrib><creatorcontrib>Huang, Jin-Xin</creatorcontrib><creatorcontrib>Fu, Jian-Ping</creatorcontrib><creatorcontrib>Peng, Yi-Yuan</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>International journal of biological macromolecules</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chai, Wei-Ming</au><au>Lin, Mei-Zhen</au><au>Song, Fang-Jun</au><au>Wang, Ying-Xia</au><au>Xu, Kai-Li</au><au>Huang, Jin-Xin</au><au>Fu, Jian-Ping</au><au>Peng, Yi-Yuan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Rifampicin as a novel tyrosinase inhibitor: Inhibitory activity and mechanism</atitle><jtitle>International journal of biological macromolecules</jtitle><addtitle>Int J Biol Macromol</addtitle><date>2017-09</date><risdate>2017</risdate><volume>102</volume><spage>425</spage><epage>430</epage><pages>425-430</pages><issn>0141-8130</issn><eissn>1879-0003</eissn><abstract>[Display omitted]
In this study, the inhibitory effect and mechanism of rifampicin on the activity of tyrosinase were investigated for developing a novel tyrosinase inhibitor. It was found to have a significant inhibition on the activity of tyrosinase (IC50=90±0.6μM). From the kinetics analysis, it was proved to be a reversible and noncompetitive type inhibitor of the enzyme with the KI value of 94±3.5μM. The results obtained from intrinsic fluorescence quenching indicated that rifampicin could interact with tyrosinase. In particular, the drastic decrease of fluorescence intensity was due to the formation of a rifampicin-enzyme complex in a static procedure which was mainly driven by hydrophobic forces and hydrogen bonding. Moreover, the ANS-binding fluorescence analysis suggested that rifampicin binding to tyrosinase changed the polarity of the hydrophobic regions. Molecular docking analysis further revealed that the hydrogen bonds were generated between rifampicin and amino residues Leu7, Ser52, and Glu107 in the B chain of the enzyme. And the hydrophobic forces produced through the interaction of rifampicin with B chain residues Pro9, Pro14, and Trp106. This work identified a novel tyrosinase inhibitor and potentially contributed to the usage of rifampicin as a potential hyperpigmentation drug.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>28414110</pmid><doi>10.1016/j.ijbiomac.2017.04.058</doi><tpages>6</tpages></addata></record> |
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| subjects | Agaricales - enzymology Enzyme Inhibitors - metabolism Enzyme Inhibitors - pharmacology Kinetics Mechanism Molecular Docking Simulation Monophenol Monooxygenase - antagonists & inhibitors Monophenol Monooxygenase - chemistry Monophenol Monooxygenase - metabolism Protein Conformation Rifampicin Rifampin - metabolism Rifampin - pharmacology Tyrosinase inhibitor |
| title | Rifampicin as a novel tyrosinase inhibitor: Inhibitory activity and mechanism |
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