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Updated: Feb 27, 2026

A Method to Study the C924T Polymorphism of the Thromboxane A2 Receptor Gene
Published on: April 1, 2019
Interactive Analysis of TX-1123 with Cyclo-oxygenase: Design of COX2 Selective TX Analogs
Kazuto Ohkura1, Yohei Tatematsu2, Yuki Kawaguchi3
1Graduate School of Pharmaceutical Sciences, Suzuka University of Medical Science Graduate School, Suzuka, Japan kohkura@suzuka-u.ac.jp.
Background:
To date, two cyclo-oxygenase (COX) isoforms, COX1 and COX2, have been identified. In the present study, the COX-inhibitory activities of TX-1123 derivatives with the 2-hydroxyarylidene-4-cyclopentene-1,3-dione structure were examined, and the binding profiles of TX-1123 to COXs were analyzed using docking simulations.
Materials And Methods:
X-Ray data on COX1 [protein data bank (PDB) ID=1PGG] and COX2 (PDB ID=3LN1) were used for molecular interactive simulations. The interactive profiles of TX-1123 derivatives with COXs were examined using a molecular simulation technique with Molegro Virtual Docker (CLC bio, Aarhus, Denmark).
Results:
TX-1123 exhibited COX1-inhibitory activity [half-maximal-inhibitory concentration (IC50)=1.57×10-5 M]. The COX2 inhibitory activity of TX-1123 was potent (IC50=1.16×10-6 M), and the ratio of COX1/COX2 inhibition was 13.5. TX-1123 bound to the COX2 molecule, and the oxygen atom of the 4-cyclopentene-1,3-dione region of TX-1123 interacted with Cys26 and Gln447 of COX2.
Conclusion:
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.
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