Synthesis and Studies of the Inhibitory Effect of Hydroxylated Phenylpropanoids and Biphenols Derivatives on Tyrosinase and Laccase Enzymes

The impaired activity of tyrosinase and laccase can provoke serious concerns in the life cycles of mammals, insects and microorganisms. Investigation of inhibitors of these two enzymes may lead to the discovery of whitening agents, medicinal products, anti-browning substances and compounds for contr...
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Autor*in:	Maria Antonietta Dettori [verfasserIn] Davide Fabbri [verfasserIn] Alessandro Dessì [verfasserIn] Roberto Dallocchio [verfasserIn] Paola Carta [verfasserIn] Claudia Honisch [verfasserIn] Paolo Ruzza [verfasserIn] Donatella Farina [verfasserIn] Rossana Migheli [verfasserIn] Pier Andrea Serra [verfasserIn] Roberto A. Pantaleoni [verfasserIn] Xenia Fois [verfasserIn] Gaia Rocchitta [verfasserIn] Giovanna Delogu [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2020

Schlagwörter:	oxidase and polyphenol oxidase polyphenols tyrosinase inhibitors chitin inhibitors SAR studies biosensors

Übergeordnetes Werk:	In: Molecules - MDPI AG, 2003, 25(2020), 11, p 2709
Übergeordnetes Werk:	volume:25 ; year:2020 ; number:11, p 2709

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3390/molecules25112709

Katalog-ID:	DOAJ003570002

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Indexfelder

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allfields	10.3390/molecules25112709 doi (DE-627)DOAJ003570002 (DE-599)DOAJ03cae88b6de24c64a2719f099fa5c023 DE-627 ger DE-627 rakwb eng QD241-441 Maria Antonietta Dettori verfasserin aut Synthesis and Studies of the Inhibitory Effect of Hydroxylated Phenylpropanoids and Biphenols Derivatives on Tyrosinase and Laccase Enzymes 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The impaired activity of tyrosinase and laccase can provoke serious concerns in the life cycles of mammals, insects and microorganisms. Investigation of inhibitors of these two enzymes may lead to the discovery of whitening agents, medicinal products, anti-browning substances and compounds for controlling harmful insects and bacteria. A small collection of novel reversible tyrosinase and laccase inhibitors with a phenylpropanoid and hydroxylated biphenyl core was prepared using naturally occurring compounds and their activity was measured by spectrophotometric and electrochemical assays. Biosensors based on tyrosinase and laccase enzymes were constructed and used to detect the type of protein-ligand interaction and half maximal inhibitory concentration (IC<sub<50</sub<). Most of the inhibitors showed an IC<sub<50</sub< in a range of 20–423 nM for tyrosinase and 23–2619 nM for laccase. Due to the safety concerns of conventional tyrosinase and laccase inhibitors, the viability of the new compounds was assayed on PC12 cells, four of which showed a viability of roughly 80% at 40 µM. In silico studies on the crystal structure of laccase enzyme identified a hydroxylated biphenyl bearing a prenylated chain as the lead structure, which activated strong and effective interactions at the active site of the enzyme. These data were confirmed by in vivo experiments performed on the insect model <i<Tenebrio molitur</i<. oxidase and polyphenol oxidase polyphenols tyrosinase inhibitors chitin inhibitors SAR studies biosensors Organic chemistry Davide Fabbri verfasserin aut Alessandro Dessì verfasserin aut Roberto Dallocchio verfasserin aut Paola Carta verfasserin aut Claudia Honisch verfasserin aut Paolo Ruzza verfasserin aut Donatella Farina verfasserin aut Rossana Migheli verfasserin aut Pier Andrea Serra verfasserin aut Roberto A. Pantaleoni verfasserin aut Xenia Fois verfasserin aut Gaia Rocchitta verfasserin aut Giovanna Delogu verfasserin aut In Molecules MDPI AG, 2003 25(2020), 11, p 2709 (DE-627)311313132 (DE-600)2008644-1 14203049 nnns volume:25 year:2020 number:11, p 2709 https://doi.org/10.3390/molecules25112709 kostenfrei https://doaj.org/article/03cae88b6de24c64a2719f099fa5c023 kostenfrei https://www.mdpi.com/1420-3049/25/11/2709 kostenfrei https://doaj.org/toc/1420-3049 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 25 2020 11, p 2709
spelling	10.3390/molecules25112709 doi (DE-627)DOAJ003570002 (DE-599)DOAJ03cae88b6de24c64a2719f099fa5c023 DE-627 ger DE-627 rakwb eng QD241-441 Maria Antonietta Dettori verfasserin aut Synthesis and Studies of the Inhibitory Effect of Hydroxylated Phenylpropanoids and Biphenols Derivatives on Tyrosinase and Laccase Enzymes 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The impaired activity of tyrosinase and laccase can provoke serious concerns in the life cycles of mammals, insects and microorganisms. Investigation of inhibitors of these two enzymes may lead to the discovery of whitening agents, medicinal products, anti-browning substances and compounds for controlling harmful insects and bacteria. A small collection of novel reversible tyrosinase and laccase inhibitors with a phenylpropanoid and hydroxylated biphenyl core was prepared using naturally occurring compounds and their activity was measured by spectrophotometric and electrochemical assays. Biosensors based on tyrosinase and laccase enzymes were constructed and used to detect the type of protein-ligand interaction and half maximal inhibitory concentration (IC<sub<50</sub<). Most of the inhibitors showed an IC<sub<50</sub< in a range of 20–423 nM for tyrosinase and 23–2619 nM for laccase. Due to the safety concerns of conventional tyrosinase and laccase inhibitors, the viability of the new compounds was assayed on PC12 cells, four of which showed a viability of roughly 80% at 40 µM. In silico studies on the crystal structure of laccase enzyme identified a hydroxylated biphenyl bearing a prenylated chain as the lead structure, which activated strong and effective interactions at the active site of the enzyme. These data were confirmed by in vivo experiments performed on the insect model <i<Tenebrio molitur</i<. oxidase and polyphenol oxidase polyphenols tyrosinase inhibitors chitin inhibitors SAR studies biosensors Organic chemistry Davide Fabbri verfasserin aut Alessandro Dessì verfasserin aut Roberto Dallocchio verfasserin aut Paola Carta verfasserin aut Claudia Honisch verfasserin aut Paolo Ruzza verfasserin aut Donatella Farina verfasserin aut Rossana Migheli verfasserin aut Pier Andrea Serra verfasserin aut Roberto A. Pantaleoni verfasserin aut Xenia Fois verfasserin aut Gaia Rocchitta verfasserin aut Giovanna Delogu verfasserin aut In Molecules MDPI AG, 2003 25(2020), 11, p 2709 (DE-627)311313132 (DE-600)2008644-1 14203049 nnns volume:25 year:2020 number:11, p 2709 https://doi.org/10.3390/molecules25112709 kostenfrei https://doaj.org/article/03cae88b6de24c64a2719f099fa5c023 kostenfrei https://www.mdpi.com/1420-3049/25/11/2709 kostenfrei https://doaj.org/toc/1420-3049 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 25 2020 11, p 2709
allfields_unstemmed	10.3390/molecules25112709 doi (DE-627)DOAJ003570002 (DE-599)DOAJ03cae88b6de24c64a2719f099fa5c023 DE-627 ger DE-627 rakwb eng QD241-441 Maria Antonietta Dettori verfasserin aut Synthesis and Studies of the Inhibitory Effect of Hydroxylated Phenylpropanoids and Biphenols Derivatives on Tyrosinase and Laccase Enzymes 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The impaired activity of tyrosinase and laccase can provoke serious concerns in the life cycles of mammals, insects and microorganisms. Investigation of inhibitors of these two enzymes may lead to the discovery of whitening agents, medicinal products, anti-browning substances and compounds for controlling harmful insects and bacteria. A small collection of novel reversible tyrosinase and laccase inhibitors with a phenylpropanoid and hydroxylated biphenyl core was prepared using naturally occurring compounds and their activity was measured by spectrophotometric and electrochemical assays. Biosensors based on tyrosinase and laccase enzymes were constructed and used to detect the type of protein-ligand interaction and half maximal inhibitory concentration (IC<sub<50</sub<). Most of the inhibitors showed an IC<sub<50</sub< in a range of 20–423 nM for tyrosinase and 23–2619 nM for laccase. Due to the safety concerns of conventional tyrosinase and laccase inhibitors, the viability of the new compounds was assayed on PC12 cells, four of which showed a viability of roughly 80% at 40 µM. In silico studies on the crystal structure of laccase enzyme identified a hydroxylated biphenyl bearing a prenylated chain as the lead structure, which activated strong and effective interactions at the active site of the enzyme. These data were confirmed by in vivo experiments performed on the insect model <i<Tenebrio molitur</i<. oxidase and polyphenol oxidase polyphenols tyrosinase inhibitors chitin inhibitors SAR studies biosensors Organic chemistry Davide Fabbri verfasserin aut Alessandro Dessì verfasserin aut Roberto Dallocchio verfasserin aut Paola Carta verfasserin aut Claudia Honisch verfasserin aut Paolo Ruzza verfasserin aut Donatella Farina verfasserin aut Rossana Migheli verfasserin aut Pier Andrea Serra verfasserin aut Roberto A. Pantaleoni verfasserin aut Xenia Fois verfasserin aut Gaia Rocchitta verfasserin aut Giovanna Delogu verfasserin aut In Molecules MDPI AG, 2003 25(2020), 11, p 2709 (DE-627)311313132 (DE-600)2008644-1 14203049 nnns volume:25 year:2020 number:11, p 2709 https://doi.org/10.3390/molecules25112709 kostenfrei https://doaj.org/article/03cae88b6de24c64a2719f099fa5c023 kostenfrei https://www.mdpi.com/1420-3049/25/11/2709 kostenfrei https://doaj.org/toc/1420-3049 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 25 2020 11, p 2709
allfieldsGer	10.3390/molecules25112709 doi (DE-627)DOAJ003570002 (DE-599)DOAJ03cae88b6de24c64a2719f099fa5c023 DE-627 ger DE-627 rakwb eng QD241-441 Maria Antonietta Dettori verfasserin aut Synthesis and Studies of the Inhibitory Effect of Hydroxylated Phenylpropanoids and Biphenols Derivatives on Tyrosinase and Laccase Enzymes 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The impaired activity of tyrosinase and laccase can provoke serious concerns in the life cycles of mammals, insects and microorganisms. Investigation of inhibitors of these two enzymes may lead to the discovery of whitening agents, medicinal products, anti-browning substances and compounds for controlling harmful insects and bacteria. A small collection of novel reversible tyrosinase and laccase inhibitors with a phenylpropanoid and hydroxylated biphenyl core was prepared using naturally occurring compounds and their activity was measured by spectrophotometric and electrochemical assays. Biosensors based on tyrosinase and laccase enzymes were constructed and used to detect the type of protein-ligand interaction and half maximal inhibitory concentration (IC<sub<50</sub<). Most of the inhibitors showed an IC<sub<50</sub< in a range of 20–423 nM for tyrosinase and 23–2619 nM for laccase. Due to the safety concerns of conventional tyrosinase and laccase inhibitors, the viability of the new compounds was assayed on PC12 cells, four of which showed a viability of roughly 80% at 40 µM. In silico studies on the crystal structure of laccase enzyme identified a hydroxylated biphenyl bearing a prenylated chain as the lead structure, which activated strong and effective interactions at the active site of the enzyme. These data were confirmed by in vivo experiments performed on the insect model <i<Tenebrio molitur</i<. oxidase and polyphenol oxidase polyphenols tyrosinase inhibitors chitin inhibitors SAR studies biosensors Organic chemistry Davide Fabbri verfasserin aut Alessandro Dessì verfasserin aut Roberto Dallocchio verfasserin aut Paola Carta verfasserin aut Claudia Honisch verfasserin aut Paolo Ruzza verfasserin aut Donatella Farina verfasserin aut Rossana Migheli verfasserin aut Pier Andrea Serra verfasserin aut Roberto A. Pantaleoni verfasserin aut Xenia Fois verfasserin aut Gaia Rocchitta verfasserin aut Giovanna Delogu verfasserin aut In Molecules MDPI AG, 2003 25(2020), 11, p 2709 (DE-627)311313132 (DE-600)2008644-1 14203049 nnns volume:25 year:2020 number:11, p 2709 https://doi.org/10.3390/molecules25112709 kostenfrei https://doaj.org/article/03cae88b6de24c64a2719f099fa5c023 kostenfrei https://www.mdpi.com/1420-3049/25/11/2709 kostenfrei https://doaj.org/toc/1420-3049 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 25 2020 11, p 2709
allfieldsSound	10.3390/molecules25112709 doi (DE-627)DOAJ003570002 (DE-599)DOAJ03cae88b6de24c64a2719f099fa5c023 DE-627 ger DE-627 rakwb eng QD241-441 Maria Antonietta Dettori verfasserin aut Synthesis and Studies of the Inhibitory Effect of Hydroxylated Phenylpropanoids and Biphenols Derivatives on Tyrosinase and Laccase Enzymes 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The impaired activity of tyrosinase and laccase can provoke serious concerns in the life cycles of mammals, insects and microorganisms. Investigation of inhibitors of these two enzymes may lead to the discovery of whitening agents, medicinal products, anti-browning substances and compounds for controlling harmful insects and bacteria. A small collection of novel reversible tyrosinase and laccase inhibitors with a phenylpropanoid and hydroxylated biphenyl core was prepared using naturally occurring compounds and their activity was measured by spectrophotometric and electrochemical assays. Biosensors based on tyrosinase and laccase enzymes were constructed and used to detect the type of protein-ligand interaction and half maximal inhibitory concentration (IC<sub<50</sub<). Most of the inhibitors showed an IC<sub<50</sub< in a range of 20–423 nM for tyrosinase and 23–2619 nM for laccase. Due to the safety concerns of conventional tyrosinase and laccase inhibitors, the viability of the new compounds was assayed on PC12 cells, four of which showed a viability of roughly 80% at 40 µM. In silico studies on the crystal structure of laccase enzyme identified a hydroxylated biphenyl bearing a prenylated chain as the lead structure, which activated strong and effective interactions at the active site of the enzyme. These data were confirmed by in vivo experiments performed on the insect model <i<Tenebrio molitur</i<. oxidase and polyphenol oxidase polyphenols tyrosinase inhibitors chitin inhibitors SAR studies biosensors Organic chemistry Davide Fabbri verfasserin aut Alessandro Dessì verfasserin aut Roberto Dallocchio verfasserin aut Paola Carta verfasserin aut Claudia Honisch verfasserin aut Paolo Ruzza verfasserin aut Donatella Farina verfasserin aut Rossana Migheli verfasserin aut Pier Andrea Serra verfasserin aut Roberto A. Pantaleoni verfasserin aut Xenia Fois verfasserin aut Gaia Rocchitta verfasserin aut Giovanna Delogu verfasserin aut In Molecules MDPI AG, 2003 25(2020), 11, p 2709 (DE-627)311313132 (DE-600)2008644-1 14203049 nnns volume:25 year:2020 number:11, p 2709 https://doi.org/10.3390/molecules25112709 kostenfrei https://doaj.org/article/03cae88b6de24c64a2719f099fa5c023 kostenfrei https://www.mdpi.com/1420-3049/25/11/2709 kostenfrei https://doaj.org/toc/1420-3049 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 25 2020 11, p 2709
language	English
source	In Molecules 25(2020), 11, p 2709 volume:25 year:2020 number:11, p 2709
sourceStr	In Molecules 25(2020), 11, p 2709 volume:25 year:2020 number:11, p 2709
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	oxidase and polyphenol oxidase polyphenols tyrosinase inhibitors chitin inhibitors SAR studies biosensors Organic chemistry
isfreeaccess_bool	true
container_title	Molecules
authorswithroles_txt_mv	Maria Antonietta Dettori @@aut@@ Davide Fabbri @@aut@@ Alessandro Dessì @@aut@@ Roberto Dallocchio @@aut@@ Paola Carta @@aut@@ Claudia Honisch @@aut@@ Paolo Ruzza @@aut@@ Donatella Farina @@aut@@ Rossana Migheli @@aut@@ Pier Andrea Serra @@aut@@ Roberto A. Pantaleoni @@aut@@ Xenia Fois @@aut@@ Gaia Rocchitta @@aut@@ Giovanna Delogu @@aut@@
publishDateDaySort_date	2020-01-01T00:00:00Z
hierarchy_top_id	311313132
id	DOAJ003570002
language_de	englisch
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author	Maria Antonietta Dettori
spellingShingle	Maria Antonietta Dettori misc QD241-441 misc oxidase and polyphenol oxidase misc polyphenols misc tyrosinase inhibitors misc chitin inhibitors misc SAR studies misc biosensors misc Organic chemistry Synthesis and Studies of the Inhibitory Effect of Hydroxylated Phenylpropanoids and Biphenols Derivatives on Tyrosinase and Laccase Enzymes
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topic_title	QD241-441 Synthesis and Studies of the Inhibitory Effect of Hydroxylated Phenylpropanoids and Biphenols Derivatives on Tyrosinase and Laccase Enzymes oxidase and polyphenol oxidase polyphenols tyrosinase inhibitors chitin inhibitors SAR studies biosensors
topic	misc QD241-441 misc oxidase and polyphenol oxidase misc polyphenols misc tyrosinase inhibitors misc chitin inhibitors misc SAR studies misc biosensors misc Organic chemistry
topic_unstemmed	misc QD241-441 misc oxidase and polyphenol oxidase misc polyphenols misc tyrosinase inhibitors misc chitin inhibitors misc SAR studies misc biosensors misc Organic chemistry
topic_browse	misc QD241-441 misc oxidase and polyphenol oxidase misc polyphenols misc tyrosinase inhibitors misc chitin inhibitors misc SAR studies misc biosensors misc Organic chemistry
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title	Synthesis and Studies of the Inhibitory Effect of Hydroxylated Phenylpropanoids and Biphenols Derivatives on Tyrosinase and Laccase Enzymes
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title_full	Synthesis and Studies of the Inhibitory Effect of Hydroxylated Phenylpropanoids and Biphenols Derivatives on Tyrosinase and Laccase Enzymes
author_sort	Maria Antonietta Dettori
journal	Molecules
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author_browse	Maria Antonietta Dettori Davide Fabbri Alessandro Dessì Roberto Dallocchio Paola Carta Claudia Honisch Paolo Ruzza Donatella Farina Rossana Migheli Pier Andrea Serra Roberto A. Pantaleoni Xenia Fois Gaia Rocchitta Giovanna Delogu
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doi_str_mv	10.3390/molecules25112709
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title_sort	synthesis and studies of the inhibitory effect of hydroxylated phenylpropanoids and biphenols derivatives on tyrosinase and laccase enzymes
callnumber	QD241-441
title_auth	Synthesis and Studies of the Inhibitory Effect of Hydroxylated Phenylpropanoids and Biphenols Derivatives on Tyrosinase and Laccase Enzymes
abstract	The impaired activity of tyrosinase and laccase can provoke serious concerns in the life cycles of mammals, insects and microorganisms. Investigation of inhibitors of these two enzymes may lead to the discovery of whitening agents, medicinal products, anti-browning substances and compounds for controlling harmful insects and bacteria. A small collection of novel reversible tyrosinase and laccase inhibitors with a phenylpropanoid and hydroxylated biphenyl core was prepared using naturally occurring compounds and their activity was measured by spectrophotometric and electrochemical assays. Biosensors based on tyrosinase and laccase enzymes were constructed and used to detect the type of protein-ligand interaction and half maximal inhibitory concentration (IC<sub<50</sub<). Most of the inhibitors showed an IC<sub<50</sub< in a range of 20–423 nM for tyrosinase and 23–2619 nM for laccase. Due to the safety concerns of conventional tyrosinase and laccase inhibitors, the viability of the new compounds was assayed on PC12 cells, four of which showed a viability of roughly 80% at 40 µM. In silico studies on the crystal structure of laccase enzyme identified a hydroxylated biphenyl bearing a prenylated chain as the lead structure, which activated strong and effective interactions at the active site of the enzyme. These data were confirmed by in vivo experiments performed on the insect model <i<Tenebrio molitur</i<.
abstractGer	The impaired activity of tyrosinase and laccase can provoke serious concerns in the life cycles of mammals, insects and microorganisms. Investigation of inhibitors of these two enzymes may lead to the discovery of whitening agents, medicinal products, anti-browning substances and compounds for controlling harmful insects and bacteria. A small collection of novel reversible tyrosinase and laccase inhibitors with a phenylpropanoid and hydroxylated biphenyl core was prepared using naturally occurring compounds and their activity was measured by spectrophotometric and electrochemical assays. Biosensors based on tyrosinase and laccase enzymes were constructed and used to detect the type of protein-ligand interaction and half maximal inhibitory concentration (IC<sub<50</sub<). Most of the inhibitors showed an IC<sub<50</sub< in a range of 20–423 nM for tyrosinase and 23–2619 nM for laccase. Due to the safety concerns of conventional tyrosinase and laccase inhibitors, the viability of the new compounds was assayed on PC12 cells, four of which showed a viability of roughly 80% at 40 µM. In silico studies on the crystal structure of laccase enzyme identified a hydroxylated biphenyl bearing a prenylated chain as the lead structure, which activated strong and effective interactions at the active site of the enzyme. These data were confirmed by in vivo experiments performed on the insect model <i<Tenebrio molitur</i<.
abstract_unstemmed	The impaired activity of tyrosinase and laccase can provoke serious concerns in the life cycles of mammals, insects and microorganisms. Investigation of inhibitors of these two enzymes may lead to the discovery of whitening agents, medicinal products, anti-browning substances and compounds for controlling harmful insects and bacteria. A small collection of novel reversible tyrosinase and laccase inhibitors with a phenylpropanoid and hydroxylated biphenyl core was prepared using naturally occurring compounds and their activity was measured by spectrophotometric and electrochemical assays. Biosensors based on tyrosinase and laccase enzymes were constructed and used to detect the type of protein-ligand interaction and half maximal inhibitory concentration (IC<sub<50</sub<). Most of the inhibitors showed an IC<sub<50</sub< in a range of 20–423 nM for tyrosinase and 23–2619 nM for laccase. Due to the safety concerns of conventional tyrosinase and laccase inhibitors, the viability of the new compounds was assayed on PC12 cells, four of which showed a viability of roughly 80% at 40 µM. In silico studies on the crystal structure of laccase enzyme identified a hydroxylated biphenyl bearing a prenylated chain as the lead structure, which activated strong and effective interactions at the active site of the enzyme. These data were confirmed by in vivo experiments performed on the insect model <i<Tenebrio molitur</i<.
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container_issue	11, p 2709
title_short	Synthesis and Studies of the Inhibitory Effect of Hydroxylated Phenylpropanoids and Biphenols Derivatives on Tyrosinase and Laccase Enzymes
url	https://doi.org/10.3390/molecules25112709 https://doaj.org/article/03cae88b6de24c64a2719f099fa5c023 https://www.mdpi.com/1420-3049/25/11/2709 https://doaj.org/toc/1420-3049
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Synthesis and Studies of the Inhibitory Effect of Hydroxylated Phenylpropanoids and Biphenols Derivatives on Tyrosinase and Laccase Enzymes

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