Cheruvallath V K, Riley C M, Narayanan S R, Lindenbaum S, Perrin J H
Dura Pharmaceuticals, San Diego, CA 92121, USA.
J Pharm Biomed Anal. 1997 Jul;15(11):1719-24. doi: 10.1016/s0731-7085(96)01956-5.
The binding constants for racemic, R and S naproxen and ibuprofen to human serum albumin have been determined by a circular dichroic technique. The ibuprofens and naproxens show no measurable extrinsic optical activity on interaction with the protein, and so the extrinsic Cotton effect shown following the diazepam-albumin interaction is used as a probe. The presence of the drugs reduce the amount of diazepam bound as shown by the interaction is used as a probe. The presence of the drugs reduce the amount of diazepam bound as shown by the reduced size of the induced ellipticity. The calculated primary binding constants show that the S form of both drugs bind to the albumin more tightly than the R form and that the racemic forms bind less tightly than either enantiomer.
已通过圆二色技术测定了消旋萘普生、R-萘普生、S-萘普生以及布洛芬与人血清白蛋白的结合常数。布洛芬和萘普生与蛋白质相互作用时未表现出可测量的外在光学活性，因此，以地西泮-白蛋白相互作用后出现的外在科顿效应作为探针。药物的存在会减少地西泮的结合量，这通过诱导椭圆率大小的减小得以体现。计算得出的一级结合常数表明，两种药物的S型比R型与白蛋白的结合更紧密，且消旋体的结合紧密程度低于任何一种对映体。
