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Specificbinding
Т. 79, № 3 ЖУРНАЛ ПРИКЛАДНОЙ СПЕКТРОСКОПИИ МАЙ — ИЮНЬ 2012
V. 79, N 3 JOURNAL OF APPLIED SPECTROSCOPY MAY — JUNE 2012
SPECIFIC BINDING OF TUBEIMOSIDE-2 WITH PROTEINS IN HEPATOCARCINOMA
HEPG2 CELLS: INVESTIGATION BY MOLECULAR SPECTROSCOPY
a b c a*
Sun Yang , Sun Shi-Sheng , Zhao Ying-Yong , Fan Jun
a School of Chemical Engineering, Northwest University,
Xi’an, Shaanxi 710069, China; e-mail: fanjun@nwu.edu.cn
b Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi’an, Shaanxi, China
c Biomedicine Key Laboratory of Shaanxi Province, Northwest University, Xi’an, China
In this study, we compared different binding interactions of TBMS2 with proteins both in hepatocarcinoma
HepG2 cells and in normal embryon hepatic L02 cells by using fluorescence, absorption, and CD spectroscopy.
The fluorescence data revealed that the fluorescence intensity of proteins in the HepG2 and L02 cells decreased in
the presence of TBMS2 by 30.79% and 12.01%, respectively. Binding constants and thermodynamic parameters
were obtained for systems of TBMS2 with the two kinds of cell proteins. The results indicated that HepG2 cell
proteins had a higher TBMS2 binding activity than those in the L02 cells. Analysis of the TBMS2 cyto toxic activi-
ties showed that TBMS2 could selectively induce apoptosis of HepG2 cells by binding to them, while its apop totic
effect on L02 cells was relatively weaker.
Keywords: tubeimoside-2, hepatocarcinoma cells, specific binding, molecular spectroscopy, cytotox icity.
ИССЛЕДОВАНИЕ СПЕЦИФИЧЕСКОГО СВЯЗЫВАНИЯ ТУБЕИМОЗИДА-2
С ПРОТЕИНАМИ КЛЕТОК ЗЛОКАЧЕСТВЕННОЙ ГЕПАТОМЫ HEPG2
МЕТОДАМИ МОЛЕКУЛЯРНОЙ СПЕКТРОСКОПИИ
a
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