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Binding of streptomycin with bovine serum albumin: energetics and conformational aspects

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Title Binding of streptomycin with bovine serum albumin: energetics and conformational aspects
 
Creator JHA, NIKI S
NAND KISHORE
 
Subject antibiotics
binding energy
calorimeters
calorimetry
circular dichroism spectroscopy
 
Description Thermodynamics of the binding of antibiotic streptomycin to bovine serum albumin have been studied using isothermal titration calorimetry in combination with fluorescence, UV–vis and circular dichroism spectroscopies. The values of van’t Hoff enthalpy calculated from the temperature dependence of the binding constant do not agree with the calorimetric enthalpies indicating temperature dependent conformational changes in the protein upon binding. With increase in the ionic strength, reduction in the binding affinity of streptomycin to BSA is observed suggesting the predominance of electrostatic interactions in the binding. The contribution of hydrophobic interactions in the binding is also demonstrated by decrease in binding affinity in the presence of tetrabutylammonium bromide (TBAB). The value of binding affinity in the presence of sucrose indicates that hydrogen bonding is not a significant contribution in complexation. The results have permitted quantitative evaluation of the interaction of streptomycin with bovine serum albumin.
 
Publisher Elsevier
 
Date 2009-09-26T08:16:15Z
2011-11-25T15:39:41Z
2011-12-26T13:05:02Z
2011-12-27T05:50:59Z
2009-09-26T08:16:15Z
2011-11-25T15:39:41Z
2011-12-26T13:05:02Z
2011-12-27T05:50:59Z
2009
 
Type Article
 
Identifier Thermochimica Acta 482(1-2), 21-29
0040-6031
http://dx.doi.org/10.1016/j.tca.2008.10.012
http://hdl.handle.net/10054/1690
http://dspace.library.iitb.ac.in/xmlui/handle/10054/1690
 
Language en