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Insights into the energetics and mechanism underlying the interaction of tetraethylammonium bromide with proteins

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Title Insights into the energetics and mechanism underlying the interaction of tetraethylammonium bromide with proteins
 
Creator BANERJEE, TUHINA
NAND KISHORE
 
Subject thermodynamic stability
differential scanning
hydrophobicity
proteins
 
Description Calorimetry has been employed to investigate the quantitative energetic aspects and mechanism underlying protein–tetraethylammonium bromide (TEAB) interactions. Differential scanning calorimetry and UV–Visible spectroscopy have been used to study the thermal unfolding of three proteins of different structure and function (bovine serum albumin, α-lactalbumin, and bovine pancreatic ribonuclease A). The mode of interaction has been studied by using isothermal titration calorimetry, which demonstrates the absence of appreciable specific binding of TEAB to the protein. This suggests the involvement of solvent mediated effects and, possibly weak non-specific binding. The thermal unfolding transitions were found to be calorimetrically reversible for α-lactalbumin and bovine pancreatic ribonuclease A and partially reversible in the case of bovine serum albumin. The results indicate protein destabilization promoted by the TEAB interaction. The preferential interaction parameters of TEAB with α-lactalbumin and ribonuclease A confirm that an increased interaction of the hydrophobic groups of the TEAB with that of the protein upon denaturation is responsible for the reduced thermal stability of the protein. The decrease in the thermal stability of proteins in the presence of TEAB is well supported by a red shift in the intrinsic fluorescence of these proteins leading to conformational change thereby shifting the native ⇌ denatured equilibrium towards right. The forces responsible for the thermal denaturation of the proteins of different structure and function in the presence of TEAB are discussed.
 
Publisher Elsevier
 
Date 2009-03-02T09:29:24Z
2011-11-25T18:18:37Z
2011-12-26T13:06:41Z
2011-12-27T05:54:42Z
2009-03-02T09:29:24Z
2011-11-25T18:18:37Z
2011-12-26T13:06:41Z
2011-12-27T05:54:42Z
2008
 
Type Article
 
Identifier The Journal of Chemical Thermodynamics 40(3), 483-491
0021-9614
http://dx.doi.org/10.1016/j.jct.2007.08.007
http://hdl.handle.net/10054/835
http://dspace.library.iitb.ac.in/xmlui/handle/10054/835
 
Language en