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人铁蛋白中银纳米颗粒的光化学还原合成。

Silver nanoparticle synthesis in human ferritin by photochemical reduction.

机构信息

Department of Chemical Engineering, Biotechnology and Materials, FCFM, University of Chile, Beauchef 851, Santiago, Chile; Center for Biotechnology and Bioengineering - CeBiB, FCFM, University of Chile, Beauchef 851, Santiago, Chile.

Department of Chemical Engineering, Biotechnology and Materials, FCFM, University of Chile, Beauchef 851, Santiago, Chile.

出版信息

J Inorg Biochem. 2020 May;206:111016. doi: 10.1016/j.jinorgbio.2020.111016. Epub 2020 Feb 1.

Abstract

Ferritin is a globular hollow protein that acts as the major iron storage protein across living organisms. The 8 nm-diameter internal cavity of ferritin has been used as a nanoreactor for the synthesis of various metallic nanoparticles different to iron oxides. For this purpose, ferritin is incubated in solution with metallic ions that enter the cavity through its natural channels. Then, these ions are subjected to a reduction step to obtain highly monodisperse metallic nanoparticles, with enhanced stability and biocompatibility provided by the ferritin structure. Potential biomedical applications of ferritin-nanoparticle complex will require the use of human ferritin to provide a safer and low-risk alternative for the delivery of metallic nanoparticles into the body. However, most of the reported protocols for metallic nanoparticles synthesis uses horse spleen ferritin as nanocontainer. Previous studies have acknowledged technical difficulties with recombinant human ferritin during the synthesis of metallic nanoparticles, like protein precipitation, which is translated into low recovery yields. In this study, we tested a novel photochemical reduction method for silver nanoparticle synthesis in human recombinant ferritin and compared it with the traditional chemical reduction method. The results show that photoreduction of silver ions inside ferritin cavity provides a universal method for silver nanoparticle synthesis in both recombinant human ferritin homopolymers (Light and Heavy ferritin). Additionally, we report important parameters that account for the efficiency of the method, such as ferritin recovery yield (~60%) and ferritin‑silver nanoparticle yield (34% for H-ferritin and 17% for L-ferritin).

摘要

铁蛋白是一种球形的中空蛋白,作为主要的铁储存蛋白存在于所有生物体中。铁蛋白的 8nm 直径的内部空腔被用作合成各种不同于氧化铁的金属纳米粒子的纳米反应器。为此,铁蛋白在溶液中与金属离子孵育,这些离子通过其天然通道进入空腔。然后,这些离子经过还原步骤,得到高度单分散的金属纳米粒子,铁蛋白结构提供了增强的稳定性和生物相容性。铁蛋白-纳米粒子复合物的潜在生物医学应用需要使用人铁蛋白,以提供一种更安全、低风险的替代方案,将金属纳米粒子递送到体内。然而,大多数报道的金属纳米粒子合成协议都使用马脾铁蛋白作为纳米容器。以前的研究已经承认在合成金属纳米粒子时,重组人铁蛋白存在技术困难,如蛋白沉淀,这导致回收率低。在这项研究中,我们测试了一种新的光化学还原方法,用于在人重组铁蛋白中合成银纳米粒子,并将其与传统的化学还原方法进行了比较。结果表明,银离子在铁蛋白空腔内的光还原为银纳米粒子的合成提供了一种通用的方法,适用于重组人铁蛋白同聚物(轻铁蛋白和重铁蛋白)。此外,我们报告了一些重要的参数,这些参数解释了该方法的效率,例如铁蛋白的回收率(~60%)和铁蛋白-银纳米粒子的产率(H 型铁蛋白为 34%,L 型铁蛋白为 17%)。

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