光谱法研究绿原酸与人血清白蛋白的相互作用

SPECTROSCOPIC STUDY ON THE INTERACTION OF CHLOROGENIC ACID AND HUMAN SERUM ALBUMIN

利用荧光光谱法研究了绿原酸与人血清白蛋白(HSA)的相互作用,考察了不同温度下绿原酸与HSA的结合常数KA和结合位点数n,并研究了Cu2+、Al3+、Ca2+、Pb2+等金属离子对绿原酸与HSA结合性质的影响。基于Frster偶极-偶极非辐射能量转移机理确定了荧光给体HSA与受体绿原酸间的结合距离。

The interaction of human serum albumin （HSA） with chlorogenic acid was studied employing fluorescence quenching and absorption spectrometric techniques. The binding of chlorogenic acid quenched the HSA fluorescence at 336 nm, which mainly originates from tryptophan residues. According to Stern - Volmer equation, the quenching style was probed. The quenching was a static quenching at lower temprature and that was a cooperative process of static and dynamic at higher temperature. The binding constant and binding sites were studied at 290,300,310,320 K, respectively. The effects of common metal ions such as Cu^2＋、Al^3＋、Ca^2＋ and Pb^2＋ on the binding of Chlorogenic acid to HSA were also studied. The main sort of acting force between chlorogenic acid and HSA was found. Based on the mechanism of the F6rster energy transference, the distance between the acceptor, chlorogenic acid, and the donor, HSA, was estimated.