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Study of the Interaction of Aglycon of Daunorubicin with Human Serum Albumin by Spectroscopy and Modeling

✍ Scribed by Fengling Cui; Lixia Qin; Guisheng Zhang; Xiaojun Yao; Beilei Lei

Publisher
John Wiley and Sons
Year
2008
Tongue
English
Weight
368 KB
Volume
8
Category
Article
ISSN
1616-5187

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✦ Synopsis

Abstract

The interaction between aglycon of daunorubicin (DNR‐A) and human serum albumin (HSA) was investigated using fluorescence quenching and modeling. Results shown that fluorescence quenching of HSA by DNR‐A resulted from the formation of DNR‐A‐HSA complex. The quenching constants were determined via measurement of the binding affinity between DNR‐A and HSA using the Stern‐Volmer equation. The thermodynamic parameters Ξ”__G__, Ξ”__H,__ Ξ”__S__ and the binding distance r were calculated. Furthermore, SFS and UV spectra suggested that the complex changed the conformation of HSA and that hydrophobic interactions played a major role in DNR‐A‐HSA association, which was in good agreement with the results of the modeling study. Moreover, the SFS technique was successfully applied to determine the total proteins in biology samples with satisfactory results.

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