柚皮苷与人血清蛋白作用机理探索

The Interaction Between Naringin and Human Serum Albumin

利用荧光光谱及同步荧光光谱法研究了柚皮苷与人血清蛋白相互作用.结果表明,相互作用使得人血清蛋白荧光猝灭且引起蛋白构象改变;猝灭常数大小证明人血清蛋白荧光猝灭机制为静态猝灭;根据能量转移原理求得结合距离为3.7 nm,存在发生能量转移的可能性.

The interaction between naringin and Human Serum Albumin （HSA） was studied by fluorescence and synchronous fluorescence spectrum. The results suggested that the fluorescence of HSA was quenched by naringin and the interaction caused change of protein conformation. The quenching constant indicated that the quenching mechanism was a static quenching process. The distance was calculated to be 3.7 nm according to the theory of the Forster energy transference.