Welcome to the UPF Digital Repository

The unravelling of the complex pattern of tyrosinase inhibition

Show simple item record

dc.contributor.author Deri, Batel
dc.contributor.author Kanteev, Margarita
dc.contributor.author Goldfeder, Mor
dc.contributor.author Lecina, Daniel
dc.contributor.author Guallar i Tasies, Víctor
dc.contributor.author Adir, Noam
dc.contributor.author Fishman, Ayelet
dc.date.accessioned 2017-01-27T08:53:32Z
dc.date.available 2017-01-27T08:53:32Z
dc.date.issued 2016
dc.identifier.citation Deri B, Kanteev M, Goldfeder M, Lecina D, Guallar i Tasies V, Adir N, Fishman A. The unravelling of the complex pattern of tyrosinase inhibition. Scientific Reports. 2016; 6: 34993. DOI: 10.1038/srep34993
dc.identifier.issn 2045-2322
dc.identifier.uri http://hdl.handle.net/10230/28005
dc.description.abstract Tyrosinases are responsible for melanin formation in all life domains. Tyrosinase inhibitors are used for the prevention of severe skin diseases, in skin-whitening creams and to avoid fruit browning, however continued use of many such inhibitors is considered unsafe. In this study we provide conclusive evidence of the inhibition mechanism of two well studied tyrosinase inhibitors, KA (kojic acid) and HQ (hydroquinone), which are extensively used in hyperpigmentation treatment. KA is reported in the literature with contradicting inhibition mechanisms, while HQ is described as both a tyrosinase inhibitor and a substrate. By visualization of KA and HQ in the active site of TyrBm crystals, together with molecular modeling, binding constant analysis and kinetic experiments, we have elucidated their mechanisms of inhibition, which was ambiguous for both inhibitors. We confirm that while KA acts as a mixed inhibitor, HQ can act both as a TyrBm substrate and as an inhibitor.
dc.format.mimetype application/pdf
dc.language.iso eng
dc.publisher Nature Publishing Group
dc.relation.ispartof Environmental Health Perspectives. 2011; 119(12): 1781-1787
dc.rights © Nature Publishing Group. This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
dc.rights.uri http://creativecommons.org/licenses/by/4.0/
dc.title The unravelling of the complex pattern of tyrosinase inhibition
dc.type info:eu-repo/semantics/article
dc.identifier.doi http://dx.doi.org/10.1038/srep34993
dc.subject.keyword Enzyme mechanisms
dc.subject.keyword X-ray crystallography
dc.rights.accessRights info:eu-repo/semantics/openAccess
dc.type.version info:eu-repo/semantics/publishedVersion

Thumbnail

This item appears in the following Collection(s)

Show simple item record

Search DSpace


Advanced Search

Browse

My Account

Statistics

In collaboration with Compliant to Partaking