Interaction of Polyethyleneimine-Functionalized ZnO Nanoparticles with Bovine Serum Albumin
Interaction of Polyethyleneimine-Functionalized ZnO Nanoparticles with Bovine Serum Albumin
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DOI：
10.1021/la3007603
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发表时间：
2012-07-31
期刊：
影响因子：
3.9
通讯作者：
Chakrabarti, Pinak
中科院分区：
文献类型：
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作者：
Chakraborti, Soumyananda;Joshi, Prachi;Chakrabarti, Pinak
在生物流体中，纳米颗粒总是被蛋白质包围。当蛋白质吸附在表面上时，吸附的程度以及对蛋白质构象和稳定性的影响取决于纳米颗粒（NP）的化学性质、形状和大小。我们进行了详细的研究牛血清白蛋白（BSA）与聚乙烯亚胺功能化的氧化锌纳米粒子（ZnO-PEI）的相互作用。ZnO-PEI使用湿化学方法合成，具有类似于3-7 nm的核尺寸（来自透射电子显微镜）。BSA与ZnO-PEI的相互作用进行了研究，使用量热，光谱和计算技术的组合。等温滴定量热法（ITC）研究了这种结合，结果表明络合是由静电驱动的，表明可能涉及静电相互作用。为了研究相互作用的性质和结合位点的位置，使用自适应Poisson-Boltzmann软件（APBS）进行详细的逐域表面静电势计算。结果表明，蛋白质表面可以结合纳米颗粒。在结合ZnO-PEI时，蛋白质在一定程度上变得不稳定，如CD（圆二色性）和FTIR（傅里叶变换红外）光谱所示。BSA的化学和热变性，当在ZnO-PEI的存在下进行，也表明在蛋白质结构的小扰动。结合的焓和熵分量与那些来自BSA与ZnO纳米粒子的相互作用的比较解释了连接在NP表面上的亲水性阳离子物种的效果。NP表面修饰对BSA结构和稳定性的影响将在纳米生物技术中找到有用的应用。
In biological fluids, nanoparticles are always surrounded by proteins. As the protein is adsorbed on the surface, the extent of adsorption and the effect on the protein conformation and stability are dependent on the chemical nature, shape, and size of the nanoparticle (NP). We have carried out a detailed investigation on the interaction of bovine serum albumin (BSA) with polyethyleneimine-functionalized ZnO nanoparticles (ZnO-PEI). ZnO-PEI was synthesized using a wet chemical method with a core size of similar to 3-7 nm (from transmission electron microscopy). The interaction of BSA with ZnO-PEI was examined using a combination of calorimetric, spectroscopic, and computational techniques. The binding was studied by ITC (isothermal titration calorimetry), and the result revealed that the complexation is enthalpy-driven, indicating the possible involvement of electrostatic interaction. To investigate the nature of the interaction and the location of the binding site, a detailed domain-wise surface electrostatic potential calculation was performed using adaptive Poisson-Boltzmann software (APBS). The result shows that the protein surface can bind the nanoparticle. On binding ZnO-PEI, the protein gets destabilized to some extent, as displayed by CD (circular dichroism) and FTIR (Fourier transform infrared) spectroscopy. Chemical and thermal denaturation of BSA, when carried out in the presence of ZnO-PEI, also indicated a small perturbation in the protein structure. A comparison of the enthalpy and entropy components of binding with those derived for the interaction of BSA with ZnO nanoparticles explains the effect of hydrophilic cationic species attached on the NP surface. The effect of the NP surface modification on the structure and stability of BSA would find useful applications in nanobiotechnology.