Please use this identifier to cite or link to this item: https://doi.org/10.21256/zhaw-19486
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dc.contributor.authorFischer, Thomas-
dc.contributor.authorKoulas, Symeon M.-
dc.contributor.authorTsagkarakou, Anastasia S.-
dc.contributor.authorKyriakis, Efthimios-
dc.contributor.authorStravodimos, George A.-
dc.contributor.authorSkamnaki, Vassiliki T.-
dc.contributor.authorLiggri, Panagiota G.V.-
dc.contributor.authorZographos, Spyros E.-
dc.contributor.authorRiedl, Rainer-
dc.contributor.authorLeonidas, Demetres D.-
dc.date.accessioned2020-02-19T14:36:20Z-
dc.date.available2020-02-19T14:36:20Z-
dc.date.issued2019-
dc.identifier.issn1420-3049de_CH
dc.identifier.issn1433-1373de_CH
dc.identifier.urihttps://digitalcollection.zhaw.ch/handle/11475/19486-
dc.description.abstractStructure-based design and synthesis of two biphenyl-N-acyl-β-d-glucopyranosylamine derivatives as well as their assessment as inhibitors of human liver glycogen phosphorylase (hlGPa, a pharmaceutical target for type 2 diabetes) is presented. X-ray crystallography revealed the importance of structural water molecules and that the inhibitory efficacy correlates with the degree of disturbance caused by the inhibitor binding to a loop crucial for the catalytic mechanism. The in silico-derived models of the binding mode generated during the design process corresponded very well with the crystallographic data.de_CH
dc.language.isoende_CH
dc.publisherMDPIde_CH
dc.relation.ispartofMoleculesde_CH
dc.rightshttp://creativecommons.org/licenses/by/4.0/de_CH
dc.subjectN-acyl-β-d-glucopyranosylaminede_CH
dc.subjectX-ray crystallographyde_CH
dc.subjectGlycogen metabolismde_CH
dc.subjectGlycogen phosphorylase inhibitorde_CH
dc.subjectStructure-based designde_CH
dc.subjectType 2 diabetesde_CH
dc.subjectBinding Sitede_CH
dc.subjectCatalytic domainde_CH
dc.subjectSynthetic chemistry techniquede_CH
dc.subjectDrug designde_CH
dc.subjectEnzyme inhibitorde_CH
dc.subjectGlucosaminede_CH
dc.subjectGlycogen phosphorylasede_CH
dc.subjectHumande_CH
dc.subjectHydrogen bondingde_CH
dc.subjectMolecular modelde_CH
dc.subjectProtein bindingde_CH
dc.subjectQuantitative structure-activity relationshipde_CH
dc.subject.ddc540: Chemiede_CH
dc.titleHigh consistency of structure-based design and x-ray crystallography : design, synthesis, kinetic evaluation and crystallographic binding mode determination of biphenyl-N-acyl-β-D-glucopyranosylamines as glycogen phosphorylase inhibitorsde_CH
dc.typeBeitrag in wissenschaftlicher Zeitschriftde_CH
dcterms.typeTextde_CH
zhaw.departementLife Sciences und Facility Managementde_CH
dc.identifier.doi10.3390/molecules24071322de_CH
dc.identifier.doi10.21256/zhaw-19486-
dc.identifier.pmid30987252de_CH
zhaw.funding.euNode_CH
zhaw.issue7de_CH
zhaw.originated.zhawYesde_CH
zhaw.pages.start1322de_CH
zhaw.publication.statuspublishedVersionde_CH
zhaw.volume24de_CH
zhaw.publication.reviewPeer review (Publikation)de_CH
zhaw.author.additionalNode_CH
Appears in collections:Publikationen Life Sciences und Facility Management

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