Assessment of new anti-HER2 ligands using combined docking, QM/MM scoring and MD simulation

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dc.AffiliationOctober University for modern sciences and Arts (MSA)
dc.contributor.authorAhmed M.
dc.contributor.authorSadek M.M.
dc.contributor.authorSerrya R.A.
dc.contributor.authorKafafy A.-H.N.
dc.contributor.authorAbouzid K.A.
dc.contributor.authorWang F.
dc.contributor.otherEChemistry Laboratory
dc.contributor.otherFaculty of Life and Social Sciences
dc.contributor.otherSwinburne University of Technology
dc.contributor.otherMelbourne
dc.contributor.otherVIC 3122
dc.contributor.otherAustralia; Pharmaceutical Organic Chemistry
dc.contributor.otherFaculty of Pharmacy
dc.contributor.otherMSA University
dc.contributor.otherEgypt; Pharmaceutical Chemistry Department
dc.contributor.otherFaculty of Pharmacy
dc.contributor.otherAin Shams University
dc.contributor.otherCairo 11566
dc.contributor.otherEgypt; Pharmaceutical Organic Chemistry Department
dc.contributor.otherFaculty of Pharmacy
dc.contributor.otherAssiut University
dc.contributor.otherEgypt
dc.date.accessioned2020-01-09T20:42:27Z
dc.date.available2020-01-09T20:42:27Z
dc.date.issued2013
dc.descriptionScopus
dc.description.abstractIn the development of new anti-cancer drugs to tackle the problem of resistance to current chemotherapeutic agents, a new series of anti-HER2 (human epidermal growth factor receptors 2) agents has been synthesized and investigated using different computational methods. Although non-selective, the most active inhibitor in the new series shows higher activity toward HER2 than EGFR. The induced fit docking protocol (IFD) is performed to find possible binding poses of the new inhibitors in the active site of the HER2 receptor. Molecular dynamic simulations of the inhibitor-protein complexes for the two most active compounds from the new series are carried out. Simulations stability is checked using different stability parameters. Different scoring functions are employed. � 2012 Elsevier Inc.en_US
dc.description.urihttps://www.scimagojr.com/journalsearch.php?q=24621&tip=sid&clean=0
dc.identifier.doihttps://doi.org/10.1016/j.jmgm.2012.12.001
dc.identifier.doiPubMed ID 23353584
dc.identifier.issn10933263
dc.identifier.otherhttps://doi.org/10.1016/j.jmgm.2012.12.001
dc.identifier.otherPubMed ID 23353584
dc.identifier.urihttps://t.ly/BXJPn
dc.language.isoEnglishen_US
dc.relation.ispartofseriesJournal of Molecular Graphics and Modelling
dc.relation.ispartofseries40
dc.subjectAMBERen_US
dc.subjectHER2en_US
dc.subjectMolecular dynamicsen_US
dc.subjectProtein kinaseen_US
dc.subjectQM/MM scoringen_US
dc.subjectActive compoundsen_US
dc.subjectActive siteen_US
dc.subjectAnticancer drugen_US
dc.subjectChemotherapeutic agentsen_US
dc.subjectHER2en_US
dc.subjectHuman epidermal growth factoren_US
dc.subjectInduced fiten_US
dc.subjectMD simulationen_US
dc.subjectProtein kinaseen_US
dc.subjectQM/MM scoringen_US
dc.subjectScoring functionsen_US
dc.subjectStability parametersen_US
dc.subjectAmberen_US
dc.subjectComputer simulationen_US
dc.subjectProteinsen_US
dc.subjectMolecular dynamicsen_US
dc.subjectepidermal growth factor receptor 2en_US
dc.subjectepidermal growth factor receptor kinase inhibitoren_US
dc.subjectarticleen_US
dc.subjectdrug activityen_US
dc.subjectdrug bindingen_US
dc.subjectdrug stabilityen_US
dc.subjectdrug structureen_US
dc.subjectdrug synthesisen_US
dc.subjectmolecular dockingen_US
dc.subjectmolecular dynamicsen_US
dc.subjectpriority journalen_US
dc.subjectscoring systemen_US
dc.subjectAntineoplastic Agentsen_US
dc.subjectDrug Designen_US
dc.subjectHumansen_US
dc.subjectLigandsen_US
dc.subjectModels, Molecularen_US
dc.subjectProtein Bindingen_US
dc.subjectQuantum Theoryen_US
dc.subjectReceptor, erbB-2en_US
dc.subjectStructure-Activity Relationshipen_US
dc.titleAssessment of new anti-HER2 ligands using combined docking, QM/MM scoring and MD simulationen_US
dc.typeArticleen_US
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