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Some aspect of the interactions of adriamycin with human serum albumin

✍ Scribed by Lilianna Trynda-Lemiesz; Henryk Kozlowski

Publisher
Elsevier Science
Year
1996
Tongue
English
Weight
388 KB
Volume
4
Category
Article
ISSN
0968-0896

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✦ Synopsis

Al~tract--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.

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