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Quantitative aspects of recognition of the antibiotic drug oxytetracycline by bovine serum albumin: Calorimetric and spectroscopic studies

Abstract

Highlights: ► Thermodynamics of oxytetracycline (OTC)-bovine serum albumin (BSA) binding addressed. ► ITC and fluorescence spectroscopic analysis provide values of binding constant. ► Binding is mainly ionic, hydrophobic with minor hydrogen bonding contribution. ► Quantitative effects of OTC on BSA stability provided by DSC. ► Preferential complexation of one domain of BSA by OTC at site II is suggested. -- Abstract: A quantitative understanding of the mode of interaction of drugs with target proteins provides a guide for the synthesis of new drug molecules. The binding of the antibiotic drug oxytetracycline with serum albumin has been studied by a combination of isothermal titration calorimetry (ITC), differential scanning calorimetry (DSC), steady-state and time-resolved fluorescence spectroscopy, and circular dichroism spectroscopy. The values of the binding constant (K), enthalpy change (ΔH), entropy (ΔS), and stoichiometry of binding have been determined along with the associated conformational changes in the protein. Oxytetracycline binds to bovine serum albumin with a 1:1 stoichiometry and with a weakly temperature dependent association constant of 1.8 · 10{sup 4} at T = 298.15 K. The effect of ionic strength, tetrabutylammonium bromide, and sucrose on the thermodynamic parameters obtained from ITC and DSC measurements indicate involvement of predominantly ionic and hydrophobic  More>>
Authors:
Keswani, Neelam; Choudhary, Sinjan; [1]  Kishore, Nand [1] 
  1. Department of Chemistry, Indian Institute of Technology Bombay, Powai, Mumbai 400 076 (India)
Publication Date:
Mar 15, 2013
Product Type:
Journal Article
Resource Relation:
Journal Name: Journal of Chemical Thermodynamics; Journal Volume: 58; Other Information: Copyright (c) 2012 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA)
Subject:
37 INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY; 60 APPLIED LIFE SCIENCES; ALBUMINS; BLOOD SERUM; CALORIMETRY; CATTLE; CONFORMATIONAL CHANGES; ENTHALPY; ENTROPY; FLUORESCENCE; FLUORESCENCE SPECTROSCOPY; HYDROGEN; INTERACTIONS; OXYTETRACYCLINE; SACCHAROSE; STABILITY; SYNTHESIS; TEMPERATURE DEPENDENCE; THERMODYNAMICS; TITRATION
OSTI ID:
22232301
Country of Origin:
United Kingdom
Language:
English
Other Identifying Numbers:
Journal ID: ISSN 0021-9614; CODEN: JCTDAF; Other: PII: S0021-9614(12)00421-1; TRN: GB14R9438053388
Availability:
Available from http://dx.doi.org/10.1016/j.jct.2012.11.006
Submitting Site:
INIS
Size:
page(s) 196-205
Announcement Date:
May 30, 2014

Citation Formats

Keswani, Neelam, Choudhary, Sinjan, and Kishore, Nand. Quantitative aspects of recognition of the antibiotic drug oxytetracycline by bovine serum albumin: Calorimetric and spectroscopic studies. United Kingdom: N. p., 2013. Web. doi:10.1016/J.JCT.2012.11.006.
Keswani, Neelam, Choudhary, Sinjan, & Kishore, Nand. Quantitative aspects of recognition of the antibiotic drug oxytetracycline by bovine serum albumin: Calorimetric and spectroscopic studies. United Kingdom. doi:10.1016/J.JCT.2012.11.006.
Keswani, Neelam, Choudhary, Sinjan, and Kishore, Nand. 2013. "Quantitative aspects of recognition of the antibiotic drug oxytetracycline by bovine serum albumin: Calorimetric and spectroscopic studies." United Kingdom. doi:10.1016/J.JCT.2012.11.006. https://www.osti.gov/servlets/purl/10.1016/J.JCT.2012.11.006.
@misc{etde_22232301,
title = {Quantitative aspects of recognition of the antibiotic drug oxytetracycline by bovine serum albumin: Calorimetric and spectroscopic studies}
author = {Keswani, Neelam, Choudhary, Sinjan, and Kishore, Nand}
abstractNote = {Highlights: ► Thermodynamics of oxytetracycline (OTC)-bovine serum albumin (BSA) binding addressed. ► ITC and fluorescence spectroscopic analysis provide values of binding constant. ► Binding is mainly ionic, hydrophobic with minor hydrogen bonding contribution. ► Quantitative effects of OTC on BSA stability provided by DSC. ► Preferential complexation of one domain of BSA by OTC at site II is suggested. -- Abstract: A quantitative understanding of the mode of interaction of drugs with target proteins provides a guide for the synthesis of new drug molecules. The binding of the antibiotic drug oxytetracycline with serum albumin has been studied by a combination of isothermal titration calorimetry (ITC), differential scanning calorimetry (DSC), steady-state and time-resolved fluorescence spectroscopy, and circular dichroism spectroscopy. The values of the binding constant (K), enthalpy change (ΔH), entropy (ΔS), and stoichiometry of binding have been determined along with the associated conformational changes in the protein. Oxytetracycline binds to bovine serum albumin with a 1:1 stoichiometry and with a weakly temperature dependent association constant of 1.8 · 10{sup 4} at T = 298.15 K. The effect of ionic strength, tetrabutylammonium bromide, and sucrose on the thermodynamic parameters obtained from ITC and DSC measurements indicate involvement of predominantly ionic and hydrophobic interactions with a minor hydrogen bonding contribution in the drug-protein complexation. The DSC results on the binding of oxytetracycline with bovine serum albumin in the absence and presence of these additives provide quantitative information on the effect of drugs on the stability of bovine serum albumin, and suggest preferential complexation of one of the domains of the protein. The results further indicate that the drug occupies binding site II on bovine serum albumin.}
doi = {10.1016/J.JCT.2012.11.006}
journal = {Journal of Chemical Thermodynamics}
volume = {58}
journal type = {AC}
place = {United Kingdom}
year = {2013}
month = {Mar}
}