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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...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer International Publishing
2014
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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. |
format | Online Article Text |
id | pubmed-4117864 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Springer International Publishing |
record_format | MEDLINE/PubMed |
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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