Spectral and Crystallographic Study of Pyridinic Analogues of Nimesulide:
Determination of the Active Form of Methanesulfonamides as COX-2 Selective
Inhibitors
Fabien Julémont
Xavier de Leval
Catherine Michaux
Jacques Damas
Caroline Charlier
François Durant
Bernard Pirotte
Jean-Michel Dogné
10.1021/jm020920n.s001
https://acs.figshare.com/articles/journal_contribution/Spectral_and_Crystallographic_Study_of_Pyridinic_Analogues_of_Nimesulide_Determination_of_the_Active_Form_of_Methanesulfonamides_as_COX-2_Selective_Inhibitors/3681408
Compound <b>7</b>, <i>N</i>-(3-phenoxy-4-pyridinyl)trifluoromethanesulfonamide, showed in vitro (whole
blood assay) a strong inhibitory activity on the two cyclooxygenase (COX) enzymes (IC<sub>50</sub>(COX-1) = 2.2 μM and IC<sub>50</sub>(COX-2) = 0.4 μM), being more active but less COX-2-selective than
nimesulide. Physicochemical studies and structural analyses indicated that the anionic
sulfonamidate species seemed to be the active form of methanesulfonamides, which optimally
interacted with the COX enzymes' active sites.
2002-10-03 00:00:00
COX
2.2 μ M
IC 50