Elucidation of binding mechanism of hydroxyurea on serum albumins by different spectroscopic studies.

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Naik KM, Kolli DB, Nandibewoor ST

Elucidation of binding mechanism of hydroxyurea on serum albumins by different spectroscopic studies.

Springerplus. 2014 Jul 15;3:360. doi: 10.1186/2193-1801-3-360. eCollection 2014.

PubMed ID

25089250 [ View in PubMed

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Abstract

OBJECTIVES: 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. CONCLUSION: This kind of study of interaction between BSA and HSA with HU would be useful in pharmaceutical industry, life sciences and clinical medicine.

DrugBank Data that Cites this Article

Drug Carriers

Drug	Carrier	Kind	Organism	Pharmacological Action	Actions
Hydroxyurea	Serum albumin	Protein	Humans	No	Binder	Details