摘要
采用荧光光谱法对24(R)-拟人参皂苷元DQ[24(R)-PDQ]与牛血清蛋白(BSA)的相互作用及机制进行了研究,并利用取代试验确定了24(R)-PDQ在BSA上的结合位点。结果表明:24(R)-PDQ与BSA在298,303,310 K下的结合常数分别为2.076×103,1.587×103,1.303×103L·mol-1;24(R)-PDQ对BSA的荧光猝灭类型为静态猝灭,主要作用力是氢键和范德华力;结合位点数近似为1,24(R)-PDQ与BSA的结合位点在BSA的SiteⅠ上。
The interaction and mechanism between bovine serum albumin （BSA） and 24（R）-pseudo sapogenin DQ[24（R）-PDQ] were studied by fluorescence spectrometry, and the binding site was confirmed by displacement experiment. The results showed the binding constants were calculated to be 2. 07610^3L·mol^-1 at 298 K, 1. 587×10^3L·mol^-1 at 303 K and 1. 303×10^3L·mol^-1 at 310 K respectively, and 24（R）-PDQ induced the intrinsic fluorescence quenching of BSA through a static quenching procedure. The predominant forces in the 24（R）- PDQ-BSA complex were hydrogen binding and Van der waals force. The number of binding sites in this binary system was approximately 1. The specific binding of 24（R）-PDQ in the vicinity of Site I of BSA was clarified.
作者
杨洁
范晓丽
林佳丽
曹旭蓉
赵二劳
YANG Jie;FAN Xiaoli;LIN Jiali;CAO Xurong;ZHAO Erlao(Department of Chemistry,Xinzhou Teachers University,Xinzhou 034000,Chin)
出处
《理化检验（化学分册）》
CAS
CSCD
北大核心
2018年第7期783-787,共5页
Physical Testing and Chemical Analysis(Part B:Chemical Analysis)
基金
山西省1331工程重点学科建设计划项目(2017)
忻州师范学院博士科研启动项目(2016)
忻州师范学院基金项目(201714)
作者简介
杨洁，博士，讲师，研究方向为天然产物化学，545431607@qq．com
