Intrinsic thermodynamics of inhibitor binding to human carbonic anhydrase IX.

Vaida Linkuvienė,Jurgita Matulienė,Vaida Juozapaitienė,Vilma Michailovienė,Jelena Jachno,Daumantas Matulis

Biochimica et Biophysica Acta (BBA) - General Subjects（2016）

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摘要

•The pKa of CA IX was determined to be 6.8, the enthalpy of protonation of CA IX was −24 kJ/mol at 25 °C.•Intrinsic binding thermodynamics – structure correlations were drawn for 40 novel CA IX inhibitors.•Affinities of the CA IX inhibitors achieved the Kd_intr of 0.01 nM and the Kd_obs of 2nM.

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关键词

Intrinsic thermodynamics of protein-ligand binding,Carbonic anhydrase,Benzenesulfonamide inhibitors,Fluorescent thermal shift assay,Isothermal titration calorimetry,Drug design

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