摘要
应用光谱方法研究了生理条件下(pH=7.40)拉米夫定与牛血清白蛋白(BSA)的相互作用.结果表明,拉米夫定对BSA产生强烈猝灭作用,其荧光猝灭过程属于静态猝灭.在295K和299 K时,拉米夫定与BSA结合常数分别为1.80×104和1.17×105L.mol-1.BSA的结合力是疏水作用力.探讨了拉米夫定对BSA构象的影响,考察了体内某些共存金属离子等对拉米夫定与BSA结合作用的影响.结果表明甘草次酸、金属离子Cu2+和Zn2+等的存在,能抑制拉米夫定与BSA的结合.
The interaction of Bovine Serum Albumin （BSA） and Lamivudine was investigated by fluorescence spectroscopy under the physiological conditions （ pH = 7.40）. It was shown that Lamivudine has a strong ability of quenching the fluorescence of BSA and the quenching mechanism is a static quenching process. The binding constants at 295 K and 299 K are 1.80× 10^4 L·mol^-1 and 1.17 × 10^5 L＇mol^-1,and the numbers of binding sites（n） are 1.04, 1.22, respectively. The distance between Lamivudine and the tryptophan residue is 2.45 nm. The imeraction is mainly driven by hydrophobic force. The effects of Larnivudine on the conformation of BSA and the effects of common etc on the binding were studied in the mean time. The results show glycyrrhetinic acid and some ions such as Cu^2 ＋ and Zn^2＋ etc can inhibit the binding.
出处
《分子科学学报》
CAS
CSCD
北大核心
2011年第5期309-313,共5页
Journal of Molecular Science
基金
国家自然科学基金资助项目(81060360)
广西科学基金资助项目(2010GXNSFA013065)
广西教育厅科研资助项目(200911MS200)
关键词
拉米夫定
牛血清白蛋白
相互作用
光谱方法
Lamivudine
Bovine Serum Albumin
interaction
spectroscopic methods
