Repozytorium
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Inne
Some aspect of the interactions of adriamycin with human serum albumin.
Autorzy
Rok wydania
1996
Czasopismo
Bioorganic and Medicinal Chemistry
Numer woluminu
4
Strony
1709-1713
DOI
10.1016/0968-0896(96)00162-9
Kolekcja
Język
Angielski
Typ publikacji
Artykuł
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.
Adres publiczny
https://doi.org/10.1016/0968-0896(96)00162-9
Strona internetowa wydawcy
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