Title: Thermodynamic benchmark study using Biacore technology
Authors: 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 #
Issue Date: May-2007
Series Title: Analytical biochemistry vol:364 issue:1 pages:67-77
Abstract: 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.
ISSN: 0003-2697
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Non-KU Leuven Association publications
× corresponding author
# (joint) last author

Files in This Item:

There are no files associated with this item.

Request a copy


All items in Lirias are protected by copyright, with all rights reserved.

© Web of science