Synthesis and structure-activity relationships of novel benzene sulfonamides with potent binding affinity for bovine carbonic anhydrase II.
This manuscript reports the identification of a novel series of mono- and bis- benzene sulfonamides with potent binding affinity for bovine carbonic anhydrase II (bCAII). These compounds exhibited nanomolar equilibrium dissociation constants with K(i)'s ranging from 4.7 to 9.3nM. All compounds were ester derivatives of the weak affinity bCAII inhibitor, 4-carboxybenzenesulfonamide. Structure-activity relationships for this novel series of compounds are discussed.
Poulsen
Sally-Ann
SA
Chemical Biology Group, Eskitis Institute for Cell and Molecular Therapies, Griffith University, Nathan Campus, Brisbane 4111, Australia. s.poulsen@griffith.edu.au
Bornaghi
Laurent F
LF
Healy
Peter C
PC
D000818:Animals; D001555:Benzene Derivatives / Q000138:chemical synthesis / Q000493:pharmacokinetics*; D001665:Binding Sites; D024402:Carbonic Anhydrase II / Q000378:metabolism*; D002417:Cattle; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008968:Molecular Conformation; D013449:Sulfonamides / Q000138:chemical synthesis / Q000493:pharmacokinetics*
D001555:Benzene Derivatives; D013449:Sulfonamides; D024402:Carbonic Anhydrase II