Benzenesulfonamide-peptide conjugates as probes for secondary binding sites near the active site of carbonic anhydrase

Libraries of N-(4-sulfamoylbenzoyl)oligoglycines terminated with different L-amino acids were screened to identify tight binding inhibitors of human carbonic anhydrase II. Inhibitors terminated with hydrophobic amino acids showed significant enhancements in binding compared to the corresponding glycine derivatives. No enhancements were observed due to polar interactions.