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

Naik KM, Kolli DB, Nandibewoor ST - Springerplus (2014)

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

View Article: PubMed Central - PubMed

Affiliation: P. G. Department of Studies in Chemistry, Karnatak University, Dharwad, 580 003 India.

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.

No MeSH data available.


Related in: MedlinePlus

Synchronous fluorescence spectra of BSA and HSA. A. Synchronous fluorescence spectra of BSA-HU: For Δλ = 60 nm. Concentration of HU: (a) 0, (b) 5, (c) 10, (d) 15, (e) 20 and (f) 25 μM. The concentration of BSA was 5.0 μM. B. Synchronous fluorescence spectra of HSA-HU: (A) For Δλ = 60 nm. Concentration of HU: (a) 0, (b) 5, (c) 10, (d) 15, (e) 20, (f) 25 and (g) 30 μM. The concentration of HSA was 5.0 μM.
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Fig8: Synchronous fluorescence spectra of BSA and HSA. A. Synchronous fluorescence spectra of BSA-HU: For Δλ = 60 nm. Concentration of HU: (a) 0, (b) 5, (c) 10, (d) 15, (e) 20 and (f) 25 μM. The concentration of BSA was 5.0 μM. B. Synchronous fluorescence spectra of HSA-HU: (A) For Δλ = 60 nm. Concentration of HU: (a) 0, (b) 5, (c) 10, (d) 15, (e) 20, (f) 25 and (g) 30 μM. The concentration of HSA was 5.0 μM.

Mentions: Synchronous fluorescence spectra provide information on the molecular environment of the fluorophore functional group. The value of Δλ i.e. difference between excitation and emission wavelengths is an important operating parameter. According to Miller (Miller 1979) when Δλ is 15 nm, synchronous fluorescence spectra indicates the changes in the microenvironment of tyrosine residues and when Δλ is 60 nm, it provides information on the microenvironment of tryptophan residues. With the unchanged concentration of the BSA, HSA and the concentration of HU increased by titration, the synchronous spectroscopy were performed at Δλ = 15 nm and Δλ = 60 nm and are shown in Figure 8 (only Δλ = 60 nm were given).Figure 8


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

Naik KM, Kolli DB, Nandibewoor ST - Springerplus (2014)

Synchronous fluorescence spectra of BSA and HSA. A. Synchronous fluorescence spectra of BSA-HU: For Δλ = 60 nm. Concentration of HU: (a) 0, (b) 5, (c) 10, (d) 15, (e) 20 and (f) 25 μM. The concentration of BSA was 5.0 μM. B. Synchronous fluorescence spectra of HSA-HU: (A) For Δλ = 60 nm. Concentration of HU: (a) 0, (b) 5, (c) 10, (d) 15, (e) 20, (f) 25 and (g) 30 μM. The concentration of HSA was 5.0 μM.
© Copyright Policy - open-access
Related In: Results  -  Collection

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Fig8: Synchronous fluorescence spectra of BSA and HSA. A. Synchronous fluorescence spectra of BSA-HU: For Δλ = 60 nm. Concentration of HU: (a) 0, (b) 5, (c) 10, (d) 15, (e) 20 and (f) 25 μM. The concentration of BSA was 5.0 μM. B. Synchronous fluorescence spectra of HSA-HU: (A) For Δλ = 60 nm. Concentration of HU: (a) 0, (b) 5, (c) 10, (d) 15, (e) 20, (f) 25 and (g) 30 μM. The concentration of HSA was 5.0 μM.
Mentions: Synchronous fluorescence spectra provide information on the molecular environment of the fluorophore functional group. The value of Δλ i.e. difference between excitation and emission wavelengths is an important operating parameter. According to Miller (Miller 1979) when Δλ is 15 nm, synchronous fluorescence spectra indicates the changes in the microenvironment of tyrosine residues and when Δλ is 60 nm, it provides information on the microenvironment of tryptophan residues. With the unchanged concentration of the BSA, HSA and the concentration of HU increased by titration, the synchronous spectroscopy were performed at Δλ = 15 nm and Δλ = 60 nm and are shown in Figure 8 (only Δλ = 60 nm were given).Figure 8

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

View Article: PubMed Central - PubMed

Affiliation: P. G. Department of Studies in Chemistry, Karnatak University, Dharwad, 580 003 India.

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.

No MeSH data available.


Related in: MedlinePlus