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《Acta Chimica Sinica》 2007-04
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Spectroscopic Investigation of the Binding of the Active Components of Apocynum venetum L. to Human Serum Albumin

SU,Zhong~(a,b) QIN,Chuan~a XIE,Meng-Xia~(*,a) LI,Jian-Dong~b WANG,Ying-Dian~a (~a Analytical & Testing Center of Beijing Normal University,Beijing 100875) (~b Institute of Grassland Sciences,Northeast Normal University,Changchun 130024)  
Quercetin (QUE),rutin (RUT) and catechin (CAT) are main active components of Apocynum venetum L.The binding mechanisms of these active components to human serum albumin (HSA) have been investigated utilizing fluorescence and UV absorption spectra.The results revealed that the fluorescence quenching arose mainly from static quenching by complex formation when the c_(QUE)/c_(HSA)≤3.5,and the pro- portion of dynamic quenching increased in higher drug concentration;while the quenching mechanism was mainly static in the drug concentration range studied for RUT.However,CAT cannot form complex with HSA.The binding site number was one for QUE and RUT,and the binding constants were (1.51±0.13)×10~5 and (0.81±0.08)×10~5 L·mol~(-1),respectively.The intrinsic fluorescence of QUE and RUT conspicuously enhanced in the presence of HSA due to excited-state proton transfer (ESPT) and it fur- ther confirmed the complex formation of HSA with QUE and RUT,individually.The UV absorption bands of QUE significantly red-shifted after interacting with HSA,which signified that the phenol group dissoci- ated during the QUE-protein binding process and the binding was driven by electrostatic force.However,the combination of RUT and HSA did not induce obvious red shift of UV absorption bands of RUT,and their binding force originated probably from the hydrogen bonding between RUT and HSA.Based on the second derivative UV absorption spectra,the binding modes of QUE and RUT were discussed.
【Fund】: 国家自然科学基金(No.30470180);; 新医药学科群(No.XK100270569);; 放射性药物教育部重点实验室开放基金.
【CateGory Index】: R914
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