کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1224905 967938 2006 4 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Isothermal titration calorimetry study of epicatechin binding to serum albumin
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
Isothermal titration calorimetry study of epicatechin binding to serum albumin
چکیده انگلیسی

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, ΔH) 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 (ΔG) 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.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Pharmaceutical and Biomedical Analysis - Volume 41, Issue 5, 28 August 2006, Pages 1602–1605
نویسندگان
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