Walji F, Rosen A, Hider R C
Department of Pharmacy, King's College, London, UK.
J Pharm Pharmacol. 1993 Jun;45(6):551-8. doi: 10.1111/j.2042-7158.1993.tb05597.x.
The ability of certain drugs to induce conformational changes in human serum albumin has been examined by differential optical rotation measurements at 233 nm. At drug:protein molar ratios ([D]/[P]) of unity, the optical rotation increased, decreased or remained the same depending on the drug used. The change in the optical rotatory dispersion (ORD) signal was investigated as a function of the drug concentration. Drug-protein interactions were relatively specific. There exists at least one, and possibly more, stable preformed high affinity sites for the binding of drugs to albumin. At low [D]/[P] ratios, the ORD titration curves suggest that the high affinity sites are conformationally labile and that the albumin molecule is flexible.
通过在233nm处进行的旋光差测量，研究了某些药物诱导人血清白蛋白构象变化的能力。在药物与蛋白质的摩尔比（[D]/[P]）为1时，旋光度根据所使用的药物而增加、降低或保持不变。研究了旋光色散（ORD）信号随药物浓度的变化。药物与蛋白质的相互作用具有相对特异性。药物与白蛋白结合至少存在一个，也可能有更多稳定的预先形成的高亲和力位点。在低[D]/[P]比时，ORD滴定曲线表明高亲和力位点在构象上不稳定，并且白蛋白分子具有柔韧性。
