Thermodynamic benchmark study using Biacore technology

摘要: Abstract A total of 22 individuals participated in this benchmark study to characterize the thermodynamics small-molecule inhibitor–enzyme interactions using Biacore instruments. Participants were provided with reagents (the enzyme carbonic anhydrase II, which was immobilized onto sensor surface, and four sulfonamide-based inhibitors) instructed collect response data from 6 36 °C. van’t Hoff enthalpies entropies calculated temperature dependence binding constants. The equilibrium dissociation thermodynamic constants determined analysis matched values isothermal titration calorimetry. These results demonstrate that immobilization surface did not alter these interactions. This also provides insights into opportunities challenges carrying out studies optical biosensors.