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Please use this identifier to cite or link to this item: https://ir.swu.ac.th/jspui/handle/123456789/14067
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dc.contributor.authorSanphanya K.
dc.contributor.authorWattanapitayakul S.K.
dc.contributor.authorPhowichit S.
dc.contributor.authorFokin V.V.
dc.contributor.authorVajragupta O.
dc.date.accessioned2021-04-05T03:33:04Z-
dc.date.available2021-04-05T03:33:04Z-
dc.date.issued2013
dc.identifier.issn0960894X
dc.identifier.other2-s2.0-84876669366
dc.identifier.urihttps://ir.swu.ac.th/jspui/handle/123456789/14067-
dc.identifier.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-84876669366&doi=10.1016%2fj.bmcl.2013.03.042&partnerID=40&md5=9a035e2d7ecf67b322e565ccf3e83e4a
dc.description.abstractWe report a novel VEGFR-2 inhibitor, developed by the back-to-front approach. Docking experiments indicated that the 3-chloromethylphenylurea motif of the lead compound occupied the back pocket of VEGFR-2 kinase. An attempt was made to enhance the binding affinity of 1 by expanding the structure to access the front pocket using a triazole linker. A library of 1,4-(disubstituted)-1H-1, 2,3-triazoles were screened in silico, and one compound (VH02) was identified with an IC50 against VEGFR-2 of 0.56 μM. VH02 showed antiangiogenic effects, inhibiting tube formation in HUVEC cells (EA.hy926) at 0.3 μM, 13 times lower than its cytotoxic dose. These enzymatic and cellular activities suggest that VH02 has potential as a lead for further optimization. © 2013 Elsevier Ltd. All rights reserved.
dc.subject6 indazolyl triazole derivative
dc.subjectangiogenesis inhibitor
dc.subjectantineoplastic agent
dc.subjectsorafenib
dc.subjecttriazole
dc.subjectunclassified drug
dc.subjectvasculotropin receptor 2
dc.subjectantiangiogenic activity
dc.subjectantineoplastic activity
dc.subjectarticle
dc.subjectbinding affinity
dc.subjectbinding site
dc.subjectcancer cell culture
dc.subjectcontrolled study
dc.subjectcytotoxicity
dc.subjectdrug structure
dc.subjectenzyme active site
dc.subjectenzyme activity
dc.subjecthuman
dc.subjecthuman cell
dc.subjecthydrogen bond
dc.subjectmolecular docking
dc.subjectprotein phosphorylation
dc.subjectAntineoplastic Agents
dc.subjectCell Line, Tumor
dc.subjectCell Proliferation
dc.subjectDose-Response Relationship, Drug
dc.subjectDrug Screening Assays, Antitumor
dc.subjectHep G2 Cells
dc.subjectHuman Umbilical Vein Endothelial Cells
dc.subjectHumans
dc.subjectIndazoles
dc.subjectMCF-7 Cells
dc.subjectModels, Molecular
dc.subjectMolecular Structure
dc.subjectPhenylurea Compounds
dc.subjectProtein Kinase Inhibitors
dc.subjectStructure-Activity Relationship
dc.subjectVascular Endothelial Growth Factor Receptor-2
dc.titleNovel VEGFR-2 kinase inhibitors identified by the back-to-front approach
dc.typeArticle
dc.rights.holderScopus
dc.identifier.bibliograpycitationBioorganic and Medicinal Chemistry Letters. Vol 23, No.10 (2013), p.2962-2967
dc.identifier.doi10.1016/j.bmcl.2013.03.042
Appears in Collections:Scopus 1983-2021

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