期刊
CELL BIOCHEMISTRY AND BIOPHYSICS
卷 70, 期 1, 页码 93-101出版社
HUMANA PRESS INC
DOI: 10.1007/s12013-014-9863-1
关键词
Ciprofloxacin (CFX); Binding parameters; Circular dichroism; Human serum albumin
资金
- Council of Scientific and Industrial Research, New Delhi
- department of Biotechnology, Govt. of India
The binding of ciprofloxacin (CFX) to human serum albumin (HSA) has been investigated by fluorescence displacement and induced circular dichroism (ICD) measurements. Displacement measurements were performed with CFX in the absence and presence of marker ligands (hemin for domain I, bilirubin for interspace of domain IA and IIA, chloroform for domain II, and diazepam for domain III) to establish CFX binding site in one of the three major domains of HSA. The primary binding site of CFX is located in site I of HSA (domain IIA) in close vicinity to the site where chloroform (CHCl3) binds. It is depicted from the decrease in quenching constant of HSA-CHCl3 system (0.02 +/- A 0.06) x 10(-3) L mol(-1) compared to HSA-CFX-CHCl3 system (0.01 +/- A 0.06) x 10(-3) L mol(-1) as obtained by the fluorescence displacement spectroscopy. Furthermore, far-UV CD results show that the binding of CFX leads to change in the helicity of HSA. The ICD results indicated that the CFX binds to the domain IIA of HSA which is in agreement with the fluorescence displacement results.
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