Comparative analysis of 10 small molecules binding to carbonic anhydrase II by different investigators using Biacore technology
Comparative analysis of 10 small molecules binding to carbonic anhydrase II by different investigators using Biacore technology
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DOI：
10.1016/j.ab.2006.08.021
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发表时间：
2006-12-01
影响因子：
2.9
通讯作者：
Myszka, David G.
中科院分区：
文献类型：
--
作者：
Papalia, Giuseppe A.;Leavitt, Stephanie;Myszka, David G.
在这项基准研究中，26 位研究人员被要求使用 Biacore 光学生物传感器表征 10 种磺酰胺抑制剂与碳酸酐酶 II 结合的动力学和亲和力。大多数参与者收集了适合 1:1 交互模型的数据，但从某些仪器获得的数据集的子集质量较差。每种化合物确定的 k(a)、k(d) 和 K-D 参数的实验误差平均分别为 34%、24% 和 37%。正如预期的那样，对于亲和力极弱和/或结合速率极快的化合物，观察到报告常数的最大变化。使用生物传感器测定的结合常数与基于溶液的滴定量热法测量良好相关。这项研究的结果让我们深入了解了使用 Biacore 技术进行小分子分析时可能会遇到的挑战以及实验变异水平。 (c) 2006 Elsevier Inc. 保留所有权利。
In this benchmark study, 26 investigators were asked to characterize the kinetics and affinities of 10 sulfonamide inhibitors binding to the enzyme carbonic anhydrase II using Biacore optical biosensors. A majority of the participants collected data that could be fit to a 1:1 interaction model, but a subset of the data sets obtained from some instruments were of poor quality. The experimental errors in the k(a), k(d), and K-D parameters determined for each of the compounds averaged 34, 24, and 37%, respectively. As expected, the greatest variation in the reported constants was observed for compounds with exceptionally weak affinity and/or fast association rates. The binding constants determined using the biosensor correlated well with solution-based titration calorimetry measurements. The results of this study provide insight into the challenges, as well as the level of experimental variation, that one would expect to observe when using Biacore technology for small molecule analyses. (c) 2006 Elsevier Inc. All rights reserved.