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What is SAR of Carbonic Anhydrase Inhibitors about?

This study used surface plasmon resonance to analyze the binding kinetics of various carbonic anhydrase inhibitors. Human and bovine carbonic anhydrase proteins were immobilized on a sensor chip. Several sulfonamide inhibitors bound strongly with dissociation constants in the low nanomolar range, while some compounds showed no binding. The inhibitors with the flattest structures and double-bonded nitrogen groups had the highest association rates and strongest binding affinities.

Author

natdempkowski

Language

EN