Wells–Dawson phosphotungstates as mushroom tyrosinase inhibitors: a speciation study

Abstract In order to elucidate the active polyoxotungstate (POT) species that inhibit fungal polyphenol oxidase (AbPPO4) in sodium citrate buffer at pH 6.8, four Wells–Dawson phosphotungstates [α/β-PV 2WVI 18O62]6− (intact form), [α 2 -PV 2WVI 17O61]10− (monolacunary), [PV 2WVI 15O56]12− (trilacunar...

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Autores principales:	Raphael Lampl, Joscha Breibeck, Nadiia I. Gumerova, Mathea Sophia Galanski, Annette Rompel
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/157b02c84fed4d0dad7e2334236be5fe
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spelling	oai:doaj.org-article:157b02c84fed4d0dad7e2334236be5fe2021-12-02T19:17:05ZWells–Dawson phosphotungstates as mushroom tyrosinase inhibitors: a speciation study10.1038/s41598-021-96491-52045-2322https://doaj.org/article/157b02c84fed4d0dad7e2334236be5fe2021-09-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-96491-5https://doaj.org/toc/2045-2322Abstract In order to elucidate the active polyoxotungstate (POT) species that inhibit fungal polyphenol oxidase (AbPPO4) in sodium citrate buffer at pH 6.8, four Wells–Dawson phosphotungstates [α/β-PV 2WVI 18O62]6− (intact form), [α 2 -PV 2WVI 17O61]10− (monolacunary), [PV 2WVI 15O56]12− (trilacunary) and [H2PV 2WVI 12O48]12− (hexalacunary) were investigated. The speciation of the POT solutions under the dopachrome assay (50 mM Na-citrate buffer, pH 6.8; L-3,4−dihydroxyphenylalanine as a substrate) conditions were determined by 183W-NMR, 31P-NMR spectroscopy and mass spectrometry. The intact Wells–Dawson POT [α/β-PV 2WVI 18O62]6− shows partial (~ 69%) disintegration into the monolacunary [α 2 -PV 2WVI 17O61]10− anion with moderate activity (K i = 9.7 mM). The monolacunary [α 2 -PV 2WVI 17O61]10− retains its structural integrity and exhibits the strongest inhibition of AbPPO4 (K i = 6.5 mM). The trilacunary POT [PV 2WVI 15O56]12− rearranges to the more stable monolacunary [α 2 -PV 2WVI 17O61]10− (~ 62%) accompanied by release of free phosphates and shows the weakest inhibition (K i = 13.6 mM). The hexalacunary anion [H2PV 2WVI 12O48]12− undergoes time-dependent hydrolysis resulting in a mixture of [H2PV 2WVI 12O48]12−, [PV 8WVI 48O184]40−, [PV 2WVI 19O69(H2O)]14− and [α 2 -PV 2WVI 17O61]10− which together leads to comparable inhibitory activity (K i = 7.5 mM) after 48 h. For the solutions of [α/β-PV 2WVI 18O62]6−, [α 2 -PV 2WVI 17O61]10− and [PV 2WVI 15O56]12− the inhibitory activity is correlated to the degree of their rearrangement to [α 2 -PV 2WVI 17O61]10−. The rearrangement of hexalacunary [H2PV 2WVI 12O48]12− into at least four POTs with a negligible amount of monolacunary anion interferes with the correlation of activity to the degree of their rearrangement to [α 2 -PV 2WVI 17O61]10−. The good inhibitory effect of the Wells–Dawson [α 2 -PV 2WVI 17O61]10− anion is explained by the low charge density of its protonated forms H x [α 2 -PV 2WVI 17O61](10−x)− (x = 3 or 4) at pH 6.8.Raphael LamplJoscha BreibeckNadiia I. GumerovaMathea Sophia GalanskiAnnette RompelNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Raphael Lampl Joscha Breibeck Nadiia I. Gumerova Mathea Sophia Galanski Annette Rompel Wells–Dawson phosphotungstates as mushroom tyrosinase inhibitors: a speciation study
description	Abstract In order to elucidate the active polyoxotungstate (POT) species that inhibit fungal polyphenol oxidase (AbPPO4) in sodium citrate buffer at pH 6.8, four Wells–Dawson phosphotungstates [α/β-PV 2WVI 18O62]6− (intact form), [α 2 -PV 2WVI 17O61]10− (monolacunary), [PV 2WVI 15O56]12− (trilacunary) and [H2PV 2WVI 12O48]12− (hexalacunary) were investigated. The speciation of the POT solutions under the dopachrome assay (50 mM Na-citrate buffer, pH 6.8; L-3,4−dihydroxyphenylalanine as a substrate) conditions were determined by 183W-NMR, 31P-NMR spectroscopy and mass spectrometry. The intact Wells–Dawson POT [α/β-PV 2WVI 18O62]6− shows partial (~ 69%) disintegration into the monolacunary [α 2 -PV 2WVI 17O61]10− anion with moderate activity (K i = 9.7 mM). The monolacunary [α 2 -PV 2WVI 17O61]10− retains its structural integrity and exhibits the strongest inhibition of AbPPO4 (K i = 6.5 mM). The trilacunary POT [PV 2WVI 15O56]12− rearranges to the more stable monolacunary [α 2 -PV 2WVI 17O61]10− (~ 62%) accompanied by release of free phosphates and shows the weakest inhibition (K i = 13.6 mM). The hexalacunary anion [H2PV 2WVI 12O48]12− undergoes time-dependent hydrolysis resulting in a mixture of [H2PV 2WVI 12O48]12−, [PV 8WVI 48O184]40−, [PV 2WVI 19O69(H2O)]14− and [α 2 -PV 2WVI 17O61]10− which together leads to comparable inhibitory activity (K i = 7.5 mM) after 48 h. For the solutions of [α/β-PV 2WVI 18O62]6−, [α 2 -PV 2WVI 17O61]10− and [PV 2WVI 15O56]12− the inhibitory activity is correlated to the degree of their rearrangement to [α 2 -PV 2WVI 17O61]10−. The rearrangement of hexalacunary [H2PV 2WVI 12O48]12− into at least four POTs with a negligible amount of monolacunary anion interferes with the correlation of activity to the degree of their rearrangement to [α 2 -PV 2WVI 17O61]10−. The good inhibitory effect of the Wells–Dawson [α 2 -PV 2WVI 17O61]10− anion is explained by the low charge density of its protonated forms H x [α 2 -PV 2WVI 17O61](10−x)− (x = 3 or 4) at pH 6.8.
format	article
author	Raphael Lampl Joscha Breibeck Nadiia I. Gumerova Mathea Sophia Galanski Annette Rompel
author_facet	Raphael Lampl Joscha Breibeck Nadiia I. Gumerova Mathea Sophia Galanski Annette Rompel
author_sort	Raphael Lampl
title	Wells–Dawson phosphotungstates as mushroom tyrosinase inhibitors: a speciation study
title_short	Wells–Dawson phosphotungstates as mushroom tyrosinase inhibitors: a speciation study
title_full	Wells–Dawson phosphotungstates as mushroom tyrosinase inhibitors: a speciation study
title_fullStr	Wells–Dawson phosphotungstates as mushroom tyrosinase inhibitors: a speciation study
title_full_unstemmed	Wells–Dawson phosphotungstates as mushroom tyrosinase inhibitors: a speciation study
title_sort	wells–dawson phosphotungstates as mushroom tyrosinase inhibitors: a speciation study
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/157b02c84fed4d0dad7e2334236be5fe
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Wells–Dawson phosphotungstates as mushroom tyrosinase inhibitors: a speciation study

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