USE OF 1-ANILINO-8-NAPHTHALENE SULFONATE AS A FLUORESCENT-PROBE IN THE INVESTIGATION OF DRUG-INTERACTIONS WITH HUMAN ALPHA-1-ACID GLYCOPROTEIN AND SERUM-ALBUMIN
USE OF 1-ANILINO-8-NAPHTHALENE SULFONATE AS A FLUORESCENT-PROBE IN THE INVESTIGATION OF DRUG-INTERACTIONS WITH HUMAN ALPHA-1-ACID GLYCOPROTEIN AND SERUM-ALBUMIN
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DOI：
10.1002/jps.2600790104
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发表时间：
1990-01-01
影响因子：
3.8
通讯作者：
TILLEMENT, JP
中科院分区：
文献类型：
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作者：
ESSASSI, D;ZINI, R;TILLEMENT, JP
我们报道了一种快速表征人血清白蛋白(HSA)和α-1-酸性糖蛋白(AAG)与药物相互作用的方法。用荧光光谱法测定了1-氨基-8-萘磺酸盐(ANS)与AAG和HSA的结合作用。荧光数据显示ANS至少与AAG上的一个位点紧密结合，其亲和常数为1.35倍。106M-1。ANS：AAG络合物的荧光被多种药物的结合所猝灭。HSA：ANS络合物的荧光猝灭表现为单一的结合部位，其亲和常数为0.72倍。106M-1。用比较平衡透析法研究了AAG和HSA与ANS或其他药物的相互作用。[14C]Ppequine被用作AAG和HSA位点标记。[14C]吡喹酮似乎共享人血清白蛋白的I位(氮丙酮)和II位(安定和布洛芬)。然而，高浓度的华法林不能取代[14C]哌喹。另一方面，棕榈酸减少，而胆红素增加了哌喹的结合力。
We report a rapid method for the characterization of the human serum albumin (HSA) and alpha-1-acid glycoprotein (AAG) interactions with drugs. The binding of 1-anillino-8-naphthalene sulfonate (ANS) to AAG and HSA was measured by fluorescence spectroscopy. Fluorescence data indicated that ANS was bound tightly to at least one site on AAG, with an affinity constant of 1.35 .times. 106 M-1. The fluorescence of an ANS:AAG complex was quenched by the binding of various drugs. Fluorescence quenching of the HSA:ANS complex showed a single site with an affinity constant of 0.72 .times. 106 M-1. The interaction of AAG and HSA with ANS or other drugs was also studied by comparative equilibrium dialysis. [14C]Pipequaline was used as an AAG and HSA site marker. [14C]Pipequaline seems to share sites I (azapropazone) and II (diazepam and ibuprofen) of HSA. However, high concentration of warfarin were unable to displace [14C]pipequaline. On the other hand, it was shown that palmitic acid decreased, whereas bilirubin increased the pipequaline binding.