Study of the interaction of aglycon of daunorubicin with human serum albumin by spectroscopy and modeling.
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 DeltaG, DeltaH, DeltaS 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.
Cui
Fengling
F
School of Chemistry and Environmental Science, Key Laboratory for Environmental Pollution Control Technology of Henan Province, Henan Normal University, Xinxiang 453007, People's Republic of China. fenglingcui@hotmail.com
Qin
Lixia
L
Zhang
Guisheng
G
Yao
Xiaojun
X
Lei
Beilei
B
D000970:Antineoplastic Agents / Q000737:chemistry*; D003630:Daunorubicin / Q000737:chemistry*; D004735:Energy Transfer; D006801:Humans; D008956:Models, Chemical; D015203:Reproducibility of Results; D012680:Sensitivity and Specificity; D012709:Serum Albumin / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet
D000970:Antineoplastic Agents; D012709:Serum Albumin; D003630:Daunorubicin