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An effective approach to prepare uniform protein-Zn~(2+) nanoparticles under mild conditions

机译：在温和条件下制备均匀的蛋白质-Zn〜（2+）纳米粒子的有效方法

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摘要

We report a novel yet simple method to prepare nanometre-sized dense and spherical protein-Zn~(2+) particles, a system useful for delivery of structurally delicate protein therapeutics. To demonstrate the preparation method, a model protein, bovine serum albumin (BSA) and zinc acetate were added to a solution of polyethylene glycol, followed by freeze-drying. Protein-Zn~(2+) particles were harvested by washing the lyophilized powder using dichloromethane or acetonitrile to remove PEG. By varying formulation parameters, such as molecular weight and concentration of PEG, particles of desired diameters can easily be obtained in the range of 30-350 nm. This paniculate system was characterized using electron microscopy, laser scattering, x-ray diffraction (XRD) and differential scanning calorimeter (DSC) for morphology, particle sizes, crystalline structure and thermal properties, respectively. The results proved that the said protem-Zn~(2+) panicles are spherical, glassy and uniform in size. For the mechanism of how the PEG continuous phase facilitates the formation of spherical protein-Zn~(2+) panicles (which are irregular in shape when formed by spray-drying), we hypothesize that freezing-induced phase separation occurred during the lav/ing process, during which the BSA-Zn~(2+) complex was 'squeezed' into each dispersed particle. For structural integrity, the protein reconstituted from the particles showed the same SEC-HPLC charts as the original samples, suggesting the particle forming process did not induce protein aggregation.
机译：我们报告了一种新颖而简单的方法来制备纳米级的致密和球形蛋白质-Zn〜（2+）颗粒，该系统可用于传递结构上精细的蛋白质治疗剂。为了说明制备方法，将模型蛋白，牛血清白蛋白（BSA）和乙酸锌添加到聚乙二醇溶液中，然后冷冻干燥。通过使用二氯甲烷或乙腈洗涤冻干粉以去除PEG，收获蛋白质-Zn〜（2+）颗粒。通过改变配方参数，例如PEG的分子量和浓度，可以容易地在30-350nm的范围内获得所需直径的颗粒。使用电子显微镜，激光散射，X射线衍射（XRD）和差示扫描量热仪（DSC）分别表征了该成丸系统的形态，粒径，晶体结构和热性能。结果表明，所述Protem-Zn〜（2+）穗为球形，玻璃状且大小均一。对于PEG连续相如何促进球形蛋白质-Zn〜（2+）穗状茎形成的机理（当通过喷雾干燥形成时形状不规则），我们假设在lav /在此过程中，BSA-Zn〜（2+）络合物被“压”入每个分散的颗粒中。对于结构完整性，从颗粒重构的蛋白质显示出与原始样品相同的SEC-HPLC图，这表明颗粒形成过程未诱导蛋白质聚集。

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