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Please use this identifier to cite or link to this item: http://doi.org/10.25358/openscience-412
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dc.contributor.authorKlein, Philipp-
dc.contributor.authorBarthels, Fabian-
dc.contributor.authorJohe, Patrick-
dc.contributor.authorWagner, Annika-
dc.contributor.authorTenzer, Stefan-
dc.contributor.authorDistler, Ute-
dc.contributor.authorLe, Thien Anh-
dc.contributor.authorSchmid, Paul-
dc.contributor.authorEngel, Volker-
dc.contributor.authorEngels, Bernd-
dc.contributor.authorHellmich, Ute-
dc.contributor.authorOpatz, Till-
dc.contributor.authorSchirmeister, Tanja-
dc.date.accessioned2020-06-23T09:41:42Z-
dc.date.available2020-06-23T11:41:42Z-
dc.date.issued2020-
dc.identifier.urihttps://openscience.ub.uni-mainz.de/handle/20.500.12030/414-
dc.description.abstractThe facile synthesis and detailed investigation of a class of highly potent protease inhibitors based on 1,4-naphthoquinones with a dipeptidic recognition motif (HN-l-Phe-l-Leu-OR) in the 2-position and an electron-withdrawing group (EWG) in the 3-position is presented. One of the compound representatives, namely the acid with EWG = CN and with R = H proved to be a highly potent rhodesain inhibitor with nanomolar affinity. The respective benzyl ester (R = Bn) was found to be hydrolyzed by the target enzyme itself yielding the free acid. Detailed kinetic and mass spectrometry studies revealed a reversible covalent binding mode. Theoretical calculations with different density functionals (DFT) as well as wavefunction-based approaches were performed to elucidate the mode of action.en_GB
dc.description.sponsorshipDFG, Open Access-Publizieren Universität Mainz / Universitätsmedizin-
dc.language.isoeng-
dc.rightsCC BYde_DE
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/-
dc.subject.ddc570 Biowissenschaftende_DE
dc.subject.ddc570 Life sciencesen_GB
dc.titleNaphthoquinones as covalent reversible inhibitors of cysteine proteases : studies on inhibition mechanism and kineticsen_GB
dc.typeZeitschriftenaufsatzde_DE
dc.identifier.doihttp://doi.org/10.25358/openscience-412-
jgu.type.dinitypearticle-
jgu.type.versionPublished versionen_GB
jgu.type.resourceText-
jgu.organisation.departmentFB 04 Medizin-
jgu.organisation.departmentFB 09 Chemie, Pharmazie u. Geowissensch.-
jgu.organisation.number7950-
jgu.organisation.number2700-
jgu.organisation.nameJohannes Gutenberg-Universität Mainz-
jgu.rights.accessrightsopenAccess-
jgu.journal.titleMolecules-
jgu.journal.volume25-
jgu.journal.issue9-
jgu.pages.alternativeArt. 2064-
jgu.publisher.year2020-
jgu.publisher.nameMDPI-
jgu.publisher.placeBasel-
jgu.publisher.urihttp://dx.doi.org/10.3390/molecules25092064-
jgu.publisher.issn1420-3049-
jgu.organisation.placeMainz-
jgu.subject.ddccode570-
opus.date.accessioned2020-06-23T09:41:42Z-
opus.date.modified2020-06-23T10:00:51Z-
opus.date.available2020-06-23T11:41:42-
opus.subject.dfgcode00-000-
opus.organisation.stringFB 04: Medizin: Institut für Immunologiede_DE
opus.organisation.stringFB 09: Chemie, Pharmazie und Geowissenschaften: Institut für Organische Chemiede_DE
opus.organisation.stringFB 09: Chemie, Pharmazie und Geowissenschaften: Institut für Pharmazie und Biochemiede_DE
opus.identifier.opusid59874-
opus.institute.number0412-
opus.institute.number0905-
opus.institute.number0910-
opus.metadataonlyfalse-
opus.type.contenttypeKeinede_DE
opus.type.contenttypeNoneen_GB
opus.affiliatedJohe, Patrick-
opus.affiliatedWagner, Annika-
opus.affiliatedTenzer, Stefan-
opus.affiliatedHellmich, Ute-
opus.affiliatedOpatz, Till-
jgu.publisher.doi10.3390/molecules25092064
jgu.organisation.rorhttps://ror.org/023b0x485
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