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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.webfeedCC Drug Discoveryde_CH
zhaw.author.additionalNode_CH
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Fischer, T., Koulas, S. M., Tsagkarakou, A. S., Kyriakis, E., Stravodimos, G. A., Skamnaki, V. T., Liggri, P. G. V., Zographos, S. E., Riedl, R., & Leonidas, D. D. (2019). High 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 inhibitors. Molecules, 24(7), 1322. https://doi.org/10.3390/molecules24071322
Fischer, T. et al. (2019) ‘High 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 inhibitors’, Molecules, 24(7), p. 1322. Available at: https://doi.org/10.3390/molecules24071322.
T. Fischer et al., “High 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 inhibitors,” Molecules, vol. 24, no. 7, p. 1322, 2019, doi: 10.3390/molecules24071322.
FISCHER, Thomas, Symeon M. KOULAS, Anastasia S. TSAGKARAKOU, Efthimios KYRIAKIS, George A. STRAVODIMOS, Vassiliki T. SKAMNAKI, Panagiota G.V. LIGGRI, Spyros E. ZOGRAPHOS, Rainer RIEDL und Demetres D. LEONIDAS, 2019. High 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 inhibitors. Molecules. 2019. Bd. 24, Nr. 7, S. 1322. DOI 10.3390/molecules24071322
Fischer, Thomas, Symeon M. Koulas, Anastasia S. Tsagkarakou, Efthimios Kyriakis, George A. Stravodimos, Vassiliki T. Skamnaki, Panagiota G.V. Liggri, Spyros E. Zographos, Rainer Riedl, and Demetres D. Leonidas. 2019. “High 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 Inhibitors.” Molecules 24 (7): 1322. https://doi.org/10.3390/molecules24071322.
Fischer, Thomas, et al. “High 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 Inhibitors.” Molecules, vol. 24, no. 7, 2019, p. 1322, https://doi.org/10.3390/molecules24071322.


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