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dc.contributor.authorHermane, Jekaterina
dc.contributor.authorEichner, Simone
dc.contributor.authorMancuso, Lena
dc.contributor.authorSchröder, Benjamin
dc.contributor.authorSasse, Florenz
dc.contributor.authorZeilinger, Carsten
dc.contributor.authorKirschning, Andreas
dc.date.accessioned2019-07-02T12:20:45Z
dc.date.available2019-07-02T12:20:45Z
dc.date.issued2019-05-29
dc.identifier.citationOrg Biomol Chem. 2019 May 29;17(21):5269-5278. doi: 10.1039/c9ob00892f.en_US
dc.identifier.issn1477-0539
dc.identifier.pmid31089638
dc.identifier.doi10.1039/c9ob00892f
dc.identifier.urihttp://hdl.handle.net/10033/621839
dc.description.abstractMutasynthetic supplementation of the AHBA blocked mutant strain of S. hygroscopicus, the geldanamycin producer, with 21 aromatic and heteroaromatic amino acids provided new nonquinoid geldanamycin derivatives. Large scale (5 L) fermentation provided four new derivatives in sufficient quantity for full structural characterisation. Among these, the first thiophene derivative of reblastatin showed strong antiproliferative activity towards several human cancer cell lines. Additionally, inhibitory effects on human heat shock protein Hsp90α and bacterial heat shock protein from H. pylori HpHtpG were observed, revealing strong displacement properties for labelled ATP and demonstrating that the ATP-binding site of Hsps is the target site for the new geldanamycin derivatives.en_US
dc.publisherRoyal Society of Chemistryen_US
dc.rightsAttribution-NonCommercial-ShareAlike 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.titleNew geldanamycin derivatives with anti Hsp properties by mutasynthesis.en_US
dc.typeArticleen_US
dc.contributor.departmentHZI,Helmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr. 7,38124 Braunschweig, Germany.en_US
dc.identifier.journalOrganic and Biomolecular Chemistryen_US
refterms.dateFOA2019-07-02T12:20:45Z
dc.source.journaltitleOrganic & biomolecular chemistry


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