阿昔洛韦与牛血清蛋白相互作用研究

STUDY ON INTERACTION BETWEEN ACYCLOVIR AND BOVINE SERUM ALBUMIN

目的研究了阿昔洛韦(ACV)与牛血清白蛋白(BSA)之间的相互作用。方法在pH为7.4的Tris-HCl缓冲液中,发现阿昔洛韦在348 nm(λex=282 nm)对牛血清白蛋白的荧光有猝灭作用。并对阿昔洛韦对牛血清白蛋白荧光猝灭的机理进行了初步探讨。结果发现在弱酸性、中性及弱碱性条件下均表现为静态猝灭。利用荧光猝灭双倒数图计算了阿昔洛韦与牛血清白蛋白之间的表观结合常数为1.48×10~4、结合位点数为1,结合位置接近于色氨酸残基,牛血清白蛋白中色氨酸残基与阿昔洛韦分子间的距离为3.138 nm。结论根据热力学参数计算确定了阿昔洛韦与牛血清白蛋白之间的主要作用力类型为疏水作用力,同时,采用同步荧光技术考察了阿昔洛韦对牛血清白蛋白构象的影响。

Objective： The interaction between Bovine Serum Albumin （BSA） and acyclovir（ACV） was investigated in detail in this paper to indicate the way of combination of ACV and BSA. Methods： It was found that the fluorescence of BSA was quenched by ACV at 348 nm （λex=282 nm）, and its relative mechanism was primarily dicussed. Results： Under the weak-acid, neutral and weak basic conditions, the interaction showed fluorescent quenching, the binding constant were 1.48×10^4 and the number of binding sites were 1 by the thermodynamics parameter. The results suggested that the interaction between ACV and BSA should be hydrophobic force in nature. Conclusion： It also proved that the fluorescence quenching reaction was happened between the interaction of the tryptophan residue of BSA and ACV. The distance between the tryptophan residue of BSA and ACV was 3.138 nm.