Analyzing a kinetic titration series using affinity biosensors
Analyzing a kinetic titration series using affinity biosensors
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DOI：
10.1016/j.ab.2005.09.034
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发表时间：
2006-02-01
影响因子：
2.9
通讯作者：
Myszka, DG
中科院分区：
文献类型：
--
作者：
Karlsson, R;Katsamba, PS;Myszka, DG
使用基于亲和力的生物传感器测量结合常数的经典方法包括在同一配体表面上测试多种分析物浓度，并在结合循环之间对表面进行再生。在此我们描述一种收集动力学结合数据的替代方法，我们称之为“动力学滴定”。这种方法包括依次注入一系列分析物浓度，无需任何再生步骤。通过模拟和实验相结合，我们表明这种方法可以像经典分析方法一样可靠。此外，动力学滴定可以比传统的数据收集方法更高效，并使我们能够全面表征分析物与难以再生的配体表面的结合情况。（c）2005爱思唯尔公司。保留所有权利。
The classical method of measuring binding constants with affinity-based biosensors involves testing several analyte concentrations over the same ligand surface and regenerating the surface between binding cycles. Here we describe an alternative approach to collecting kinetic binding data, which we call "kinetic titration." This method involves sequentially injecting an analyte concentration series without any regeneration steps. Through a combination of simulation and experimentation, we show that this method can be as robust as the classical method of analysis. In addition, kinetic titrations can be more efficient than the conventional data collection method and allow us to fully characterize analyte binding to ligand surfaces that are difficult to regenerate. (c) 2005 Elsevier Inc. All rights reserved.