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