51. Probing the interaction of ferrocene containing hyperbranched poly-ester with model plasma protein: Effect on the interaction mechanism and conformational change
- Author
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Xiangfeng Wu, Fengjuan Xiao, Muqing Gu, Ye Liang, Lanlan Li, and Xiaolei Yu
- Subjects
Conformational change ,Circular dichroism ,biology ,Chemistry ,Hydrogen bond ,Biophysics ,Analytical chemistry ,General Chemistry ,Condensed Matter Physics ,Photochemistry ,Biochemistry ,Binding constant ,Fluorescence ,Atomic and Molecular Physics, and Optics ,symbols.namesake ,Electron transfer ,symbols ,biology.protein ,van der Waals force ,Bovine serum albumin - Abstract
Interaction mechanism and conformational change of model plasma protein - bovine serum albumin (BSA) induced by ferrocenyl-functionalized hyperbranched polyester (HBPE-Fc) were investigated using cyclicvoltammetry (CV), differential pulsed voltammetry (DPV), fluorescence, UV–vis absorption spectrometry and circular dichroism (CD). Some complicated interactions occurred between BSA and HBPE-Fc and the new redox centers appeared in the BSA/HBPE-Fc complex that changed and hindered the electron transfer of Fe/Fe 2+ . Fluorescence quenching data showed that the fluorescence of BSA was statically quenched by HBPE-Fc, which implied that ground state complex formed between BSA and HBPE-Fc. van der Waals force and hydrogen bond played major roles in the interaction of HBPE-Fc with BSA. The binding constant Ka for HBPE-Fc–protein interaction is in the order of 10 6 at room temperature indicates that there is a strong interaction between HBPE-Fc and BSA. Synchronous, three-dimensional fluorescence and CD studies indicated that the interaction of BSA with HBPE-Fc induced conformational changes in BSA with overall decrease in the α-helical structure and increase in β-pleated sheet structure. The molecular model of the interaction between HBPE-Fc and BSA was also presented according to the results in this study.
- Published
- 2014