SPECTROSCOPIC ANALYSIS OF THE BINDING OF DOXORUBICIN TO HUMAN ALPHA-1-ACID GLYCOPROTEIN

被引：62

作者：

HUSAIN, N ^{[1
]}

AGBARIA, RA ^{[1
]}

WARNER, IM ^{[1
]}

机构：

[1] LOUISIANA STATE UNIV,DEPT CHEM,BATON ROUGE,LA 70803

来源：

JOURNAL OF PHYSICAL CHEMISTRY | 1993年 / 97卷 / 41期

关键词：

D O I：

10.1021/j100143a054

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

The binding of the anticancer drug doxorubicin (DOX) to human alpha-1 acid glycoprotein (AGP) is investigated using absorbance and fluorescence spectroscopies. Steady-state fluorescence and UV-vis absorbance measurements produced evidence of the formation of a 1:1 complex between DOX and AGP. Scatchard analysis indicated the presence of one major binding site for the drug on the protein, and estimated complex formation constants using both spectroscopic methods ranged from 10(4) to 10(5) M-1. Fluorescence lifetime and polarization measurements provided further evidence of complexion and indicated a ''loose'' binding of DOX to its binding site on AGP. Stern-Volmer fluorescence quenching analysis showed reduced accessibility of bound DOX to an anionic quencher, suggesting that the binding site for DOX on AGP is hydrophobic in nature.

引用

页码：10857 / 10861

页数：5

共 31 条

[1] ABSORPTION, FLUORESCENCE AND RESONANCE RAMAN-SPECTRA OF ADRIAMYCIN AND ITS COMPLEX WITH DNA [J].