کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1404893 | 1501726 | 2015 | 9 صفحه PDF | دانلود رایگان |
• (+)-Catechin-BSA system is driven by enthalpy and entropy.
• (+)-Catechin can quench the fluorescence of BSA through a static quenching.
• (+)-Catechin can be stored and carried by serum albumin to reach its target organ.
• Binding site I is the primary binding site for (+)-catechin.
• (+)-Catechin may induce conformational and microenvironmental changes of BSA.
In this study, the interaction between (+)-catechin and bovine serum albumin (BSA) was investigated using isothermal titration calorimetry (ITC), in combination with fluorescence spectroscopy, UV–vis absorption spectroscopy, and Fourier transform infrared (FT-IR) spectroscopy. Thermodynamic investigations reveal that the electrostatic interaction and hydrophobic interaction are the major binding forces in the binding of (+)-catechin to BSA. The binding of (+)-catechin to BSA is synergistically driven by enthalpy and entropy. Fluorescence experiments suggest that (+)-catechin can quench the fluorescence of BSA through a static quenching mechanism. The obtained binding constants and the equilibrium fraction of unbound (+)-catechin show that (+)-catechin can be stored and transported from the circulatory system to reach its target organ. Binding site I is found to be the primary binding site for (+)-catechin. Additionally, as shown by the UV–vis absorption, synchronous fluorescence spectroscopy and FT-IR, (+)-catechin may induce conformational and microenvironmental changes of BSA.
Figure optionsDownload as PowerPoint slide
Journal: Journal of Molecular Structure - Volume 1091, 5 July 2015, Pages 109–117