Analytical biochemistry · 2007
Thermodynamic benchmark study using Biacore technology.
Сравнительное исследованиеОценочное исследованиеСтатьяМногоцентровое исследованиеВалидационное исследованиеНазвание и аннотация: Перевод в очереди
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Navratilova Iva, Papalia Giuseppe A, Rich Rebecca L, Bedinger Daniel, Brophy Susan, Condon Brad, Deng Ta, Emerick Anne W, Guan Hann-Wen, Hayden Tanya, Heutmekers Thomas, Hoorelbeke Bart, McCroskey Mark C, Murphy Mary M, Nakagawa Terry, Parmeggiani Fabio, Qin Xiaochun, Rebe Sabina, Tomasevic Nenad, Tsang Tiffany, Waddell M Brett, Zhang Fred Feiyu, Leavitt Stephanie, Myszka David G
Аннотация
A total of 22 individuals participated in this benchmark study to characterize the thermodynamics of small-molecule inhibitor-enzyme interactions using Biacore instruments. Participants were provided with reagents (the enzyme carbonic anhydrase II, which was immobilized onto the sensor surface, and four sulfonamide-based inhibitors) and were instructed to collect response data from 6 to 36 degrees C. van't Hoff enthalpies and entropies were calculated from the temperature dependence of the binding constants. The equilibrium dissociation and thermodynamic constants determined from the Biacore analysis matched the values determined using isothermal titration calorimetry. These results demonstrate that immobilization of the enzyme onto the sensor surface did not alter the thermodynamics of these interactions. This benchmark study also provides insights into the opportunities and challenges in carrying out thermodynamic studies using optical biosensors.