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

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...

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Detalles Bibliográficos
Autores principales: Naik, Keerti M, Kolli, Deepa B, Nandibewoor, Sharanappa T
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer International Publishing 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4117864/
https://www.ncbi.nlm.nih.gov/pubmed/25089250
http://dx.doi.org/10.1186/2193-1801-3-360
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author Naik, Keerti M
Kolli, Deepa B
Nandibewoor, Sharanappa T
author_facet Naik, Keerti M
Kolli, Deepa B
Nandibewoor, Sharanappa T
author_sort Naik, Keerti M
collection PubMed
description 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.
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spelling pubmed-41178642014-08-01 Elucidation of binding mechanism of hydroxyurea on serum albumins by different spectroscopic studies Naik, Keerti M Kolli, Deepa B Nandibewoor, Sharanappa T Springerplus Research 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. Springer International Publishing 2014-07-15 /pmc/articles/PMC4117864/ /pubmed/25089250 http://dx.doi.org/10.1186/2193-1801-3-360 Text en © Naik et al.; licensee Springer. 2014 This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited.
spellingShingle Research
Naik, Keerti M
Kolli, Deepa B
Nandibewoor, Sharanappa T
Elucidation of binding mechanism of hydroxyurea on serum albumins by different spectroscopic studies
title Elucidation of binding mechanism of hydroxyurea on serum albumins by different spectroscopic studies
title_full Elucidation of binding mechanism of hydroxyurea on serum albumins by different spectroscopic studies
title_fullStr Elucidation of binding mechanism of hydroxyurea on serum albumins by different spectroscopic studies
title_full_unstemmed Elucidation of binding mechanism of hydroxyurea on serum albumins by different spectroscopic studies
title_short Elucidation of binding mechanism of hydroxyurea on serum albumins by different spectroscopic studies
title_sort elucidation of binding mechanism of hydroxyurea on serum albumins by different spectroscopic studies
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4117864/
https://www.ncbi.nlm.nih.gov/pubmed/25089250
http://dx.doi.org/10.1186/2193-1801-3-360
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