In silico design: Extended molecular dynamic simulations of a new series of dually acting inhibitors against EGFR and HER2

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dc.AffiliationOctober University for modern sciences and Arts (MSA)
dc.contributor.authorAhmed M.
dc.contributor.authorSadek M.M.
dc.contributor.authorAbouzid K.A.
dc.contributor.authorWang F.
dc.contributor.otherChemistry Laboratory
dc.contributor.otherFaculty of Life and Social Sciences
dc.contributor.otherSwinburne University of Technology
dc.contributor.otherHawthorn
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
dc.date.accessioned2020-01-09T20:42:28Z
dc.date.available2020-01-09T20:42:28Z
dc.date.issued2013
dc.descriptionScopus
dc.description.abstractBased on the hit structures that have been identified in our previous studies against EGFR and HER2, new potential inhibitors that share the same scaffold of the hit structures are designed and screened in silico. Insights into understanding the potential inhibitory effect of the new inhibitors against both EGFR and HER2 receptors is obtained using extended molecular dynamics (MD) simulations and different scoring techniques. The binding mechanisms and dynamics are detailed with respect to two approved inhibitors against EGFR (lapatinib) and HER2 (SYR127063). The best scoring inhibitor (T9) is chosen for additional in silico investigation against both the wild-type and T790M mutant strain of EGFR and the wild-type HER2. The results reveal that certain substitution patterns increase the stability and assure stronger binding and higher H-bond occupancy of the conserved water molecule that is commonly observed with kinase crystal structures. Furthermore, the new inhibitor (T9) forms stable interactions with the mutant strain as a direct consequence of the enhanced ability to form additional hydrogen bonding interactions with binding site residues. 2013 Elsevier Ltd. All rights reserved.en_US
dc.identifier.doihttps://doi.org/10.1016/j.jmgm.2013.06.004
dc.identifier.doiPubMed ID 23911931
dc.identifier.issn10933263
dc.identifier.otherhttps://doi.org/10.1016/j.jmgm.2013.06.004
dc.identifier.otherPubMed ID 23911931
dc.identifier.urihttps://t.ly/ndwze
dc.language.isoEnglishen_US
dc.publisherElsevier Inc.en_US
dc.relation.ispartofseriesJournal of Molecular Graphics and Modelling
dc.relation.ispartofseries44
dc.subjectOctober University for Modern Sciences and Arts
dc.subjectجامعة أكتوبر للعلوم الحديثة والآداب
dc.subjectUniversity of Modern Sciences and Arts
dc.subjectMSA University
dc.subjectAM1-Den_US
dc.subjectEGFR/HER2en_US
dc.subjectMolecular dynamicsen_US
dc.subjectTyrosine kinaseen_US
dc.subjectWater occupancyen_US
dc.subjectAmino acidsen_US
dc.subjectBinsen_US
dc.subjectEnzymesen_US
dc.subjectHydrogen bondsen_US
dc.subjectMoleculesen_US
dc.subjectScaffoldsen_US
dc.subjectBinding mechanismsen_US
dc.subjectEGFR/HER2en_US
dc.subjectHydrogen bonding interactionsen_US
dc.subjectMolecular dynamics simulationsen_US
dc.subjectPotential inhibitorsen_US
dc.subjectScoring techniquesen_US
dc.subjectSubstitution patternsen_US
dc.subjectTyrosine kinaseen_US
dc.subjectMolecular dynamicsen_US
dc.subjectepidermal growth factor receptor kinase inhibitoren_US
dc.subjecterlotiniben_US
dc.subjectgefitiniben_US
dc.subjectlapatiniben_US
dc.subjectprotein tyrosine kinase inhibitoren_US
dc.subjectquinazoline derivativeen_US
dc.subjectsyr 127063en_US
dc.subjectunclassified drugen_US
dc.subjectarticleen_US
dc.subjectbinding siteen_US
dc.subjectcrystal structureen_US
dc.subjecthydrogen bonden_US
dc.subjectmolecular dynamicsen_US
dc.subjectnonhumanen_US
dc.subjectpriority journalen_US
dc.subjectsimulationen_US
dc.subjectAM1-Den_US
dc.subjectEGFR/HER2en_US
dc.subjectMolecular dynamicsen_US
dc.subjectTyrosine kinaseen_US
dc.subjectWater occupancyen_US
dc.subjectBinding Sitesen_US
dc.subjectComputer Simulationen_US
dc.subjectDrug Designen_US
dc.subjectHumansen_US
dc.subjectLigandsen_US
dc.subjectMolecular Conformationen_US
dc.subjectMolecular Docking Simulationen_US
dc.subjectMolecular Dynamics Simulationen_US
dc.subjectProtein Bindingen_US
dc.subjectProtein Kinase Inhibitorsen_US
dc.subjectQuantitative Structure-Activity Relationshipen_US
dc.subjectReceptor, Epidermal Growth Factoren_US
dc.subjectReceptor, erbB-2en_US
dc.subjectWateren_US
dc.titleIn silico design: Extended molecular dynamic simulations of a new series of dually acting inhibitors against EGFR and HER2en_US
dc.typeArticleen_US
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