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Isothermal titration calorimetry study of epicatechin binding to serum albumin

Frazier, R., Papadopoulou, A. and Green, R. (2006) Isothermal titration calorimetry study of epicatechin binding to serum albumin. Journal of Pharmaceutical and Biomedical Analysis , 41 (5). pp. 1602-1605. ISSN 0731-7085

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To link to this article DOI: 10.1016/j.jpba.2006.02.004

Abstract/Summary

The interaction of epicatechin with bovine serum albumin (BSA) was studied by isothermal titration calorimetry. The binding constant (K) and associated thermodynamic binding parameters (n, Delta H) were determined for the interaction at three solution concentrations of BSA using a binding model assuming independent binding sites. These data show weak non-covalent binding of epicatechin to BSA. The interaction energetics varied with BSA concentration in the calorimeter cell, suggesting that the binding of epicatechin induced BSA aggregation. The free energy (Delta G) remained constant within a range of 2 kJ mol(-1) and negative entropy was observed, indicating an enthalpy driven exothermic interaction. It is concluded that the non-covalent epicatechin-BSA complex is formed by hydrogen bonding. (c) 2006 Elsevier B.V. All rights reserved.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > School of Pharmacy > Pharmaceutics Research Group
Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Food and Nutritional Sciences > Food and Bioprocessing Research Group
Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Food and Nutritional Sciences
ID Code:13410
Uncontrolled Keywords:isothermal titration calorimetry, epicatechin, albumin, protem-polyphenol interaction, NONCOVALENT COMPLEXES, ANTIOXIDANT ACTIVITY, PROTEIN COMPLEXES, MICROCALORIMETRY, METABOLISM, FLAVONOIDS, PRECIPITATION, POLYPHENOLS, ABSORPTION, PROCYANIDIN
Publisher:Elsevier

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