Ranjan Shivendu, Dasgupta Nandita, Srivastava Priyanka, Ramalingam Chidambaram
Nano-food Research Group, Instrumental and Food Analysis Laboratory, Industrial Biotechnology Division, School of BioSciences and Technology, VIT University, Vellore, Tamil Nadu, India.
Nano-food Research Group, Instrumental and Food Analysis Laboratory, Industrial Biotechnology Division, School of BioSciences and Technology, VIT University, Vellore, Tamil Nadu, India.
J Photochem Photobiol B. 2016 Aug;161:472-81. doi: 10.1016/j.jphotobiol.2016.06.015. Epub 2016 Jun 11.
The use of nanoparticles in food or pharma requires a molecular-level perceptive of how NPs interact with protein corona once exposed to a physiological environment. In this study, the conformational changes of bovine serum albumin (BSA) were investigated in detail when exposed to different concentration of titanium dioxide nanoparticle by various techniques. To analyze the effects of NPs on proteins, the interaction between bovine serum albumin and titanium dioxide nanoparticles at different concentrations were investigated. The interaction, BSA conformations, kinetics, and adsorption were analyzed by dynamic light scattering, Fourier transform infrared spectroscopy and fluorescence quenching. Dynamic light scattering analysis confirms the interaction with major changes in the size of the protein. Fluorescence quenching analysis confirms the side-on or end-on interaction of 1.1 molecules of serum albumin to titanium dioxide nanoparticles. Further, pseudo-second order kinetics was determined with equilibrium contact time of 20min. The spectroscopic analysis suggests that there is a conformational change both at secondary and tertiary structure levels. A distortion in both α-helix and β-sheets was observed by Fourier transform infrared (FTIR) spectroscopy. Fluorescence quenching analysis confirms the interaction of a molecule of bovine serum albumin to the single TiO2 nanoparticle. Further, pseudo-second order kinetics was determined with equilibrium contact time of 20min. The data of the present study determines the detailed evaluation of BSA adsorption on TiO2 nanoparticle along with mechanism and adsorption kinetics.
在食品或制药领域使用纳米颗粒，需要从分子层面了解纳米颗粒暴露于生理环境后如何与蛋白质冠层相互作用。在本研究中，运用多种技术详细研究了牛血清白蛋白（BSA）在暴露于不同浓度二氧化钛纳米颗粒时的构象变化。为分析纳米颗粒对蛋白质的影响，研究了不同浓度下牛血清白蛋白与二氧化钛纳米颗粒之间的相互作用。通过动态光散射、傅里叶变换红外光谱和荧光猝灭分析了相互作用、BSA构象、动力学和吸附情况。动态光散射分析证实了相互作用以及蛋白质大小的主要变化。荧光猝灭分析证实了血清白蛋白的1.1个分子与二氧化钛纳米颗粒存在侧面或端面相互作用。此外，确定了伪二级动力学，平衡接触时间为20分钟。光谱分析表明，二级和三级结构水平均发生了构象变化。傅里叶变换红外（FTIR）光谱观察到α-螺旋和β-折叠均出现扭曲。荧光猝灭分析证实了一个牛血清白蛋白分子与单个TiO₂纳米颗粒的相互作用。此外，确定了伪二级动力学，平衡接触时间为20分钟。本研究数据确定了对BSA在TiO₂纳米颗粒上的吸附、吸附机制和吸附动力学的详细评估。
