Some aspect of the interactions of adriamycin with human serum albumin.
The interaction of adriamycin with human serum albumin (HSA) has been studied by absorption, CD, fluorescence spectroscopy, and quantitative precipitating HSA-antibody test. Our results demonstrate that adriamycin react with HSA and the binding to the protein molecule has a very distinct influence on the stability of ADR in aqueous solutions. The drug molecule binds protein as a monomer. The structural studies have shown the conformational change of HSA modified by adriamycin. The binding of ADR lowers the helicity of the native protein of ca. 15% and ca. 10% in the case of acHSA. The quantitative precipitating test supports distinct changes in the conformation upon ADR binding that decreases the ability of HSA to precipitate with its antibody.
Trynda-Lemiesz
L
L
Faculty of Chemistry, University of Wroclaw, Poland.
Kozlowski
H
H
D002942:Circular Dichroism; D004317:Doxorubicin / Q000378:metabolism*; D006801:Humans; D011487:Protein Conformation; D012709:Serum Albumin / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013054:Spectrophotometry, Atomic
D012709:Serum Albumin; D004317:Doxorubicin