Interactive Analysis of TX-1123 with Cyclo-oxygenase: Design of COX2 Selective TX Analogs

Ohkura, Kazuto; Tatematsu, Yohei; Kawaguchi, Yuki; Uto, Yoshihiro; Hori, Hitoshi

doi:10.21873/anticanres.11764

Cited by 1 publication

(2 citation statements)

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“…An interactive analysis of TX-2036 derivatives with the protein kinase domain of EGFR was performed using Molegro Virtual Docker (CLC bio., Aarhus, Denmark) as preciously described (8,9). The ligand-bindable pockets of the protein kinase domain of EGFR were examined using the Molegro Virtual Docker (CLC bio., Aarhus, Denmark).…”

Section: Methodsmentioning

confidence: 99%

“…In developing an anticancer drug, it is more efficient to use parameters based on dynamic structural information than to search only for biological activity. Thus far, we reported the use of three-dimensional hydrophobic parameter (dGW) and electrostatic potential field (ESP) in molecular design (4,6,7,9,12). In the present study, we considered the influence of the bulkiness of the structure attached to the pharmacophore through the structural analysis of TX-2036 derivatives.…”

Section: Interaction Between Tx-2036 Derivatives and Tyrosine Kinase ...mentioning

confidence: 99%

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Effect of Isomerization of TX-2036 Derivatives on the Interaction With Tyrosine Kinase Domain of EGF Receptor

et al. 2020

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Background: From the design and synthesis of enantiomers, we can expect to obtain two compounds with different pharmacokinetics and pharmacological activities at the same time, which is thought to lead to the development of efficient anticancer agents. Chiral-2-nitroimidazole TX-2036 derivatives exhibit stereo-configuration (R-and S-configuration)dependent tyrosine kinase inhibitory activity, and the activity of the tyrosine kinase domain of EGF receptor (EGFR-tyk) is suppressed. In order to clarify the reason why the effects on EGFR-tyk activity differ depending on stereoisomers, we tried to analyze the interaction between each TX-2036 derivative and EGFR-tyk. Materials and Methods:The 2-nitroimidazole-based radiosensitizer TX-2036 series were synthesized and their molecular features were examined using protein kinase inhibition assay and molecular structural analysis. Results: R-configured

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Section: Methodsmentioning

confidence: 99%

Section: Interaction Between Tx-2036 Derivatives and Tyrosine Kinase ...mentioning

confidence: 99%

Effect of Isomerization of TX-2036 Derivatives on the Interaction With Tyrosine Kinase Domain of EGF Receptor

et al. 2020

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Interactive Analysis of TX-1123 with Cyclo-oxygenase: Design of COX2 Selective TX Analogs

Abstract: The TX-1123-binding pocket of COX2 differs from that of the COX2-selective celecoxib-binding pocket. TX-1123 exhibited a different COX2-interactive mechanism from that of celecoxib.

Cited by 1 publication

References 4 publications

Effect of Isomerization of TX-2036 Derivatives on the Interaction With Tyrosine Kinase Domain of EGF Receptor

Effect of Isomerization of TX-2036 Derivatives on the Interaction With Tyrosine Kinase Domain of EGF Receptor

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