title: Elucidation of binding mechanism of hydroxyurea on serum albumins by different spectroscopic studies.
abstract: OBJECTIVE
  The interaction of hydroxyurea (HU) with serum albumins (SAs) has not been investigated so far. However, it necessitates the interaction study of HU with SAs in phosphate buffer of pH 7.4.
  
  
  METHODS
  The binding of HU on bovine serum albumin (BSA) and human serum albumin (HSA) was studied in vitro under simulated physiological conditions by spectroscopic methods viz., fluorescence, FT-IR, UV-vis absorption, synchronous fluorescence and three-dimensional fluorescence.
  
  
  RESULTS
  The Stern-Volmer plot indicated the presence of dynamic quenching mechanism in the interaction of HU with SAs. The number of binding sites, n and binding constants, K were obtained at various temperatures according to the double logarithm regression curve. The result of FT-IR spectra, UV-vis absorption, synchronous fluorescence and three-dimensional fluorescence spectra showed that the conformation of SAs has been changed in the presence of HU. The thermodynamic parameters were calculated according to van't Hoff equation and discussed.
  
  
  CONCLUSIONS
  This kind of study of interaction between BSA and HSA with HU would be useful in pharmaceutical industry, life sciences and clinical medicine.
authors.affiliation: P. G. Department of Studies in Chemistry, Karnatak University, Dharwad, 580 003 India.
authors.forename: Keerti M
authors.initials: KM
authors.lastname: Naik
authors.affiliation: P. G. Department of Studies in Chemistry, Karnatak University, Dharwad, 580 003 India.
authors.forename: Deepa B
authors.initials: DB
authors.lastname: Kolli
authors.affiliation: P. G. Department of Studies in Chemistry, Karnatak University, Dharwad, 580 003 India.
authors.forename: Sharanappa T
authors.initials: ST
authors.lastname: Nandibewoor
keywords: Bovine serum albumin; Fluorescence; Human serum albumin; Hydroxyurea
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