title: Some aspect of the interactions of adriamycin with human serum albumin.
abstract: 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.
authors.affiliation: Faculty of Chemistry, University of Wroclaw, Poland.
authors.forename: L
authors.initials: L
authors.lastname: Trynda-Lemiesz
authors.forename: H
authors.initials: H
authors.lastname: Kozlowski
mesh_terms: D002942:Circular Dichroism; D004317:Doxorubicin / Q000378:metabolism*; D006801:Humans; D011487:Protein Conformation; D012709:Serum Albumin / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013054:Spectrophotometry, Atomic
chemical_list: D012709:Serum Albumin; D004317:Doxorubicin