Research of the interaction between kangai injection and human serum albumin by fluorescence spectroscopy

被引:0
|
作者
Ye, Changbin [1 ]
Lin, Xiaogang [1 ]
Zhu, Hao [1 ]
Li, Wenchao [1 ]
Wu, Jie [2 ]
机构
[1] Chongqing Univ, Minist Educ China, Key Lab Optoelect Technol & Syst, Chongqing 400044, Peoples R China
[2] Univ Tennessee, Dept Elect Engn & Comp Sci, Knoxville, TN 37996 USA
来源
AOPC 2015: ADVANCED DISPLAY TECHNOLOGY; AND MICRO/NANO OPTICAL IMAGING TECHNOLOGIES AND APPLICATIONS | 2015年 / 9672卷
关键词
Kangai; Human serum albumin (HSA); Fluorescence spectroscopy; UV-Vis absorption spectroscopy; Traditional Chinese medicines; Tumor treatment; BINDING;
D O I
10.1117/12.2202788
中图分类号
TM [电工技术]; TN [电子技术、通信技术];
学科分类号
0808 ; 0809 ;
摘要
The interaction between drugs and serum albumin is the theoretical basis of pharmacology research. Kangai injection with invigorating Qi, enhancing the immune function, is widely used for a variety of malignant tumor treatment. Fluorescence spectroscopy was adopted due to its high sensitivity and other advantages. The interaction between kangai injection and human serum albumin (HSA) in physiological buffer (pH 7.4) was investigated by fluorescence spectroscopy and UV-Vis absorption spectroscopy. The results of fluorescence spectrum at three temperature (296K, 303K and 310K) showed the degree of binding at 310K is the highest. Also, the maximum emission peak has a slight blue shift, which indicates that the interaction between kangai injection and HSA has an effect on the conformation of HSA. That is, the microenvironment of tryptophan increase hydrophobic due to the increase of the concentration of kangai injection. Results obtained from analysis of fluorescence spectrum and fluorescence intensity indicated that kangai injection has a strong ability to quench the intrinsic fluorescence of HSA. And according to the Stern-Volume equation, the quenching mechanism is static quenching, which is further proved by the UV-Vis absorption spectroscopy.
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页数:6
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