Ferrer J M, Leiton M J, Zatón A M
Departamento de Bioquímica y Biología Molecular, Facultad de Farmacia, Universidad del País Vasco, Vitoria, Spain.
J Protein Chem. 1998 Feb;17(2):115-9. doi: 10.1023/a:1022575315391.
The binding of several benzopyranes to serum albumin was studied by equilibrium dialysis at pH 7.4 in a 67 mM sodium phosphate buffer at 37 degrees C. The equilibrium data were analyzed using a computer program for curve fitting. The binding isotherm for warfarin, 4-hydroxycoumarin, 4-chromanol, coumarin, 3-acetylcoumarin, and benzoic acid can be described by two stoichiometric dissociation constants. Elimination of the 4-hydroxyl group in the coumarin chemical structures decreases the binding affinity of the compounds on the primary binding site of serum albumin, with 4-chromanol the smallest ligand which binds to seroalbumin with high affinity. Thus, the affinity of 4-benzopyranol and the 4-hydroxybenzopyranones greater than that of benzopyranones. On the other hand, elimination of the 2-oxo group in the benzopyranone chemical structures decreases affinity for the secondary binding site.
在37℃的67mM磷酸钠缓冲液中，于pH 7.4条件下，通过平衡透析研究了几种苯并吡喃与血清白蛋白的结合情况。使用计算机程序进行曲线拟合来分析平衡数据。华法林、4-羟基香豆素、4-色满醇、香豆素、3-乙酰香豆素和苯甲酸的结合等温线可用两个化学计量解离常数来描述。香豆素化学结构中4-羟基的消除降低了化合物在血清白蛋白主要结合位点上的结合亲和力，4-色满醇是与血清白蛋白结合亲和力最高的最小配体。因此，4-苯并吡喃醇和4-羟基苯并吡喃酮的亲和力大于苯并吡喃酮。另一方面，苯并吡喃酮化学结构中2-氧代基团的消除降低了对次要结合位点的亲和力。
