کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1411369 | 1501859 | 2009 | 4 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
A calorimetric study on interactions of colchicine with human serum albumin
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آلی
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چکیده انگلیسی
Interaction of colchicine (COL) with human serum albumin (HSA) in buffer solutions (pH 7.2) has been investigated by isothermal titration calorimetry (ITC) combined with circular dichroism (CD) and UV-vis spectra. Heats of the interactions have been determined at 298.15Â K. Based on the calorimetric data and reasonable suppositions for the bio-macromolecule - ligand binding process, the equilibrium constants, standard changes of enthalpy, entropy and Gibbs free energy of the processes are obtained. The results show that there are two classes of ligand binding sites. The first-class binding is mainly driven by entropy, while the second-class binding is synergistically driven by entropy and enthalpy. Circular dichroism (CD) and UV-vis spectra show that COL can change the secondary structure of HSA molecule.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Molecular Structure - Volume 931, Issues 1â3, 14 August 2009, Pages 31-34
Journal: Journal of Molecular Structure - Volume 931, Issues 1â3, 14 August 2009, Pages 31-34
نویسندگان
Qiang Zhao, Xiang-Yu Xu, Xiang-Jun Sun, Min Liu, De-Zhi Sun, Lin-Wei Li,