Mohanty Abhinav, Parida Akankshika, Raut Rohit Kumar, Behera Rabindra K
Department of Chemistry, National Institute of Technology, Rourkela 769008, Odisha, India.
ACS Bio Med Chem Au. 2022 Mar 1;2(3):258-281. doi: 10.1021/acsbiomedchemau.2c00003. eCollection 2022 Jun 15.
The essence of bionanotechnology lies in the application of nanotechnology/nanomaterials to solve the biological problems. Quantum dots and nanoparticles hold potential biomedical applications, but their inherent problems such as low solubility and associated toxicity due to their interactions at nonspecific target sites is a major concern. The self-assembled, thermostable, ferritin protein nanocages possessing natural iron scavenging ability have emerged as a potential solution to all the above-mentioned problems by acting as nanoreactor and nanocarrier. Ferritins, the cellular iron repositories, are hollow, spherical, symmetric multimeric protein nanocages, which sequester the excess of free Fe(II) and synthesize iron biominerals (FeO·HO) inside their ∼5-8 nm central cavity. The electrostatics and dynamics of the pore residues not only drives the natural substrate Fe inside ferritin nanocages but also uptakes a set of other metals ions/counterions during synthesis of nanomaterial. The current review aims to report the recent developments/understanding on ferritin structure (self-assembly, surface/pores electrostatics, metal ion binding sites) and chemistry occurring inside these supramolecular protein cages (protein mediated metal ion uptake and mineralization/nanoparticle formation) along with its surface modification to exploit them for various nanobiotechnological applications. Furthermore, a better understanding of ferritin self-assembly would be highly useful for optimizing the incorporation of nanomaterials the disassembly/reassembly approach. Several studies have reported the successful engineering of these ferritin protein nanocages in order to utilize them as potential nanoreactor for synthesizing/incorporating nanoparticles and as nanocarrier for delivering imaging agents/drugs at cell specific target sites. Therefore, the combination of nanoscience (nanomaterials) and bioscience (ferritin protein) projects several benefits for various applications ranging from electronics to medicine.
生物纳米技术的核心在于应用纳米技术/纳米材料来解决生物学问题。量子点和纳米颗粒具有潜在的生物医学应用价值，但其固有问题，如溶解度低以及由于在非特异性靶点部位相互作用而产生的相关毒性，是一个主要关注点。具有天然铁清除能力的自组装、热稳定的铁蛋白蛋白质纳米笼，作为纳米反应器和纳米载体，已成为解决上述所有问题的潜在方案。铁蛋白作为细胞内的铁储存库，是中空的、球形的、对称的多聚体蛋白质纳米笼，它能螯合过量的游离Fe(II)，并在其约5 - 8纳米的中央腔内合成铁生物矿物质(FeO·HO)。孔残基的静电作用和动力学不仅驱动天然底物铁进入铁蛋白纳米笼，还在纳米材料合成过程中摄取一系列其他金属离子/抗衡离子。本综述旨在报告关于铁蛋白结构（自组装、表面/孔静电、金属离子结合位点）以及这些超分子蛋白质笼内发生的化学过程（蛋白质介导的金属离子摄取和矿化/纳米颗粒形成）的最新进展/认识，以及其表面修饰，以便将它们用于各种纳米生物技术应用。此外，更好地理解铁蛋白自组装对于优化通过拆卸/重新组装方法掺入纳米材料将非常有用。多项研究报告了这些铁蛋白蛋白质纳米笼的成功工程改造，以便将它们用作合成/掺入纳米颗粒的潜在纳米反应器，以及用作在细胞特异性靶点部位递送成像剂/药物的纳米载体。因此，纳米科学（纳米材料）和生物科学（铁蛋白蛋白质）的结合为从电子学到医学的各种应用带来了诸多益处。
