Probing the interaction of ferrocene containing hyperbranched poly-ester with model plasma protein: Effect on the interaction mechanism and conformational change

作者：Xiao, Fengjuan^*; Gu, Muqing; Liang, Ye; Li, Lanlan; Yu, Xiaolei; Wu, Xiangfeng

来源：Journal of Luminescence, 2014, 149: 306-312.

DOI：10.1016/j.jlumin.2014.01.033

• Ferrocenyl-functionalized hyperbranched polyester
• Interaction mechanism
• Conformational change
• Model plasma protein
• Fluorescence
• Circular dichroism

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/Fe2 . 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 106 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 alpha-helical structure and increase in beta-pleated sheet structure. The molecular model of the interaction between HBPE-Fc and BSA was also presented according to the results in this study.

• 出版日期2014-5