Characterizing a drug's primary binding site on albumin
Characterizing a drug's primary binding site on albumin
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DOI：
10.1002/jps.10293
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发表时间：
2003-02-01
影响因子：
3.8
通讯作者：
Myszka, DG
中科院分区：
文献类型：
--
作者：
Day, YSN;Myszka, DG
基于表面等离子体共振的生物传感器可用于直接测量小分子与白蛋白的结合。我们研究了12种具有不同分子量和白蛋白亲和力的药物，以说明该技术的好处。为了检查蛋白质上的高亲和力和低亲和力位点，在10，000倍浓度范围内测定每种药物。从生物传感器测定确定的亲和常数对应于通过其他方法确定的亲和力。我们扩大了效用的生物传感器技术的开发协议，以表征药物从白蛋白的位移。最后，我们还比较了一组具有代表性的药物如何与14个物种的白蛋白结合。这些结果说明了生物传感器如何提供有关药物在白蛋白上的主要结合位点的识别和亲和力的详细信息。(C)2003 Wiley-Liss，Inc.和美国制药协会。
Surface plasmon resonance-based biosensors can be used to directly measure the binding of small molecules to albumin. We studied 12 drugs with different molecular masses and affinities for albumin to illustrate the benefits of the technology. To examine both high- and low-affinity sites on the protein, each drug was assayed across a 10,000-fold concentration range. The affinity constants determined from the biosensor assay corresponded with affinities determined by other methods. We expanded the utility of the biosensor technology by developing protocols to characterize drug displacement from albumin. Finally, we also compared how a representative panel of drugs bound albumins from 14 species. The results illustrate how biosensors can provide detailed information about the identification and affinity of a drug's primary binding site on albumin. (C) 2003 Wiley-Liss, Inc. and the American Pharmaceutical Association.