修饰肽的重组人重链铁蛋白（FTH1）的高效表达。
Efficient expression of recombinant human heavy chain ferritin (FTH1) with modified peptides.
作者信息
Guo Jun, Xu Nuo, Yao Yao, Lin Jian, Li Riyong, Li Jiang-Wei
机构信息
Xinjiang Key Laboratory of Biological Resources and Genetic Engineering, College of Life Science and Technology, Xinjiang University, 14 Shengli Rd., Urumqi, 830046, China.
Synthetic and Functional Biomolecules Center, College of Chemistry and Molecular Engineering, Peking University, Beijing, China.
出版信息
Protein Expr Purif. 2017 Mar;131:101-108. doi: 10.1016/j.pep.2016.06.003. Epub 2016 Dec 21.
Human heavy chain ferritin (FTH1) can self-assemble into a diameter of 12-nm spherical cage with an interior cavity of 8 nm in diameter. FTH1 has great potential as a nanocage in molecular imaging and drug delivery. Different peptides have been fused with FTH1 for targeting delivery; however, the expression of FTH1 modified with peptides in soluble form is not equivalent to natural FTH1. As shown in recent study, a novel scaffold protein --thioredoxin from the archaebacterium Pyrococcus furiosus (PfTrx)--exhibits a superior solubilization capacity and thermal stability [19]. Here we report a new construct (FTH1-PfTrx-His) that can be easily expressed and purified in Escherichia coli. Of note, different peptides inserted into FTH1-PfTrx-His did not influence the expression of proteins. Finally, the doxorubicin packaging ability of FTH1-PfTrx-His is comparable to natural FTH1. Our results showed that FTH1-PfTrx-His had a potential role as a novel peptide-modified ferritin carrier for drugs or imaging probes.
人重链铁蛋白（FTH1）可自组装成直径为12纳米的球形笼，其内部空腔直径为8纳米。FTH1作为分子成像和药物递送中的纳米笼具有巨大潜力。不同的肽已与FTH1融合用于靶向递送；然而，以可溶形式用肽修饰的FTH1的表达与天然FTH1并不等同。如最近的研究所示，一种新型支架蛋白——来自嗜热栖热菌的硫氧还蛋白（PfTrx）——具有卓越的增溶能力和热稳定性[19]。在此，我们报道了一种新构建体（FTH1-PfTrx-His），它能够在大肠杆菌中轻松表达和纯化。值得注意的是，插入到FTH1-PfTrx-His中的不同肽不会影响蛋白质的表达。最后，FTH1-PfTrx-His的阿霉素包装能力与天然FTH1相当。我们的结果表明，FTH1-PfTrx-His作为一种新型的肽修饰铁蛋白载体，在药物或成像探针方面具有潜在作用。
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