Li Zhao, Hage David S
Department of Chemistry, University of Nebraska, Lincoln, NE, USA.
Department of Chemistry, University of Nebraska, Lincoln, NE, USA.
J Pharm Biomed Anal. 2017 Sep 10;144:12-24. doi: 10.1016/j.jpba.2017.01.026. Epub 2017 Jan 11.
The interactions of drugs with serum proteins are often stereoselective and can affect the distribution, activity, toxicity and rate of excretion of these drugs in the body. A number of approaches based on affinity chromatography, and particularly high-performance affinity chromatography (HPAC), have been used as tools to study these interactions. This review describes the general principles of affinity chromatography and HPAC as related to their use in drug binding studies. The types of serum agents that have been examined with these methods are also discussed, including human serum albumin, α-acid glycoprotein, and lipoproteins. This is followed by a description of the various formats based on affinity chromatography and HPAC that have been used to investigate drug interactions with serum proteins and the historical development for each of these formats. Specific techniques that are discussed include zonal elution, frontal analysis, and kinetic methods such as those that make use of band-broadening measurements, peak decay analysis, or ultrafast affinity extraction.
药物与血清蛋白的相互作用通常具有立体选择性，并且会影响这些药物在体内的分布、活性、毒性及排泄速率。基于亲和色谱，尤其是高效亲和色谱（HPAC）的一些方法已被用作研究这些相互作用的工具。本综述描述了亲和色谱和HPAC与它们在药物结合研究中的应用相关的一般原理。还讨论了用这些方法检测过的血清介质类型，包括人血清白蛋白、α-酸性糖蛋白和脂蛋白。接下来描述了基于亲和色谱和HPAC用于研究药物与血清蛋白相互作用的各种形式以及每种形式的历史发展。所讨论的具体技术包括区带洗脱、前沿分析以及动力学方法，如利用谱带展宽测量、峰衰减分析或超快速亲和萃取的方法。
