The interaction between drugs and human serum albumin (HSA) was investigated by capillary electrophoresis (CE). It involves stereoselectivity, drug displacement and synergism effects. Under protein-drug binding equilibrium, the unbound concentrations of drug enantiomers were measured by frontal anal
Study of the interaction between ofloxacin and human serum albumin by spectroscopic methods
✍ Scribed by Aurica Varlan; Sorana Ionescu; Mihaela Hillebrand
- Publisher
- John Wiley and Sons
- Year
- 2011
- Tongue
- English
- Weight
- 396 KB
- Volume
- 26
- Category
- Article
- ISSN
- 1522-7235
- DOI
- 10.1002/bio.1302
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✦ Synopsis
ABSTRACT
The binding of ofloxacin (OFLX) to human serum albumin (HSA) was investigated by fluorescence and circular dichroism (CD) techniques. The binding parameters have been evaluated by a fluorescence quenching method. Competitive binding measurements were performed in the presence of warfarin and ibuprofen and suggest binding to the warfarin site I of HSA. The distance r between donor (HSA) and acceptor (OFLX) was estimated according to the Forster's theory of non‐radiatiative energy transfer. CD spectra revealed that the binding of OFLX to HSA induced conformational changes in HSA. Molecular docking was performed and shows that for the lowest energy complex OFLX is located in site I of HSA, which correlate to the competitive binding experiments. Copyright © 2011 John Wiley & Sons, Ltd.
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