Gratton G, Decorte E, Moimas F, Angeli C, Sunjić V
Farmaco Sci. 1985 Mar;40(3):209-17.
By combining the gel filtration and circular dichroism (CD) methods in studying the binding of chiral (S)/(R)-(I) to human serum albumin (HSA) the following results were obtained: HSA affinity for (S)-(I) is about 17 times higher than for (R)-(I); there exist two independent and nonequivalent binding sites for (S)-(I), and one site of lower affinity for (R)-(I); at equimolar concentrations of (I) and HSA, (S)-enantiomer is bound up to 45%, but (R)-enantiomer binds up to 22% only; differential CD-spectra at various concentrations, in the presence of HSA at 1.45 X 10(-5) M concentration, reveals distortions of the chromophoric system i.e. of the conformation of (S)-(I). This effect, and the low affinity of both enantiomers for HSA, allows only a qualitative interpretation of CD-data.
通过结合凝胶过滤和圆二色性（CD）方法来研究手性（S）/（R）-（I）与人血清白蛋白（HSA）的结合，得到了以下结果：HSA对（S）-（I）的亲和力比对（R）-（I）高约17倍；（S）-（I）存在两个独立且不等价的结合位点，而（R）-（I）有一个亲和力较低的位点；在（I）和HSA等摩尔浓度下，（S）-对映体的结合率高达45%，但（R）-对映体仅结合至22%；在1.45×10⁻⁵ M浓度的HSA存在下，不同浓度的差异CD光谱显示发色团系统即（S）-（I）的构象发生了扭曲。这种效应以及两种对映体对HSA的低亲和力，使得对CD数据只能进行定性解释。
