Abstract
In the design of high-affinity enzyme inhibitors we have applied an approach of augmenting the substituents attached to the inhibitor benzenesulfonamide scaffold. The increased size of the substituents led to compounds of increased affinity until the spatial limitation was reached leading to an abrupt drop in affinities. This approach could be used to design compounds that are selective only toward one isoform of the carbonic anhydrase enzyme family. Such an approach, based on the Lock-and-Key principle could be used for the development of enzyme-specific compounds and provide insight into the principles of protein-ligand recognition.
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