title: Efficient expression of recombinant human heavy chain ferritin (FTH1) with modified peptides.
abstract: 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.
authors.affiliation: Xinjiang Key Laboratory of Biological Resources and Genetic Engineering, College of Life Science and Technology, Xinjiang University, 14 Shengli Rd., Urumqi, 830046, China.
authors.forename: Jun
authors.initials: J
authors.lastname: Guo
authors.affiliation: Synthetic and Functional Biomolecules Center, College of Chemistry and Molecular Engineering, Peking University, Beijing, China.
authors.forename: Nuo
authors.initials: N
authors.lastname: Xu
authors.affiliation: Department of Pharmacy, Women & Infants Hospital of Zhengzhou, Zhengzhou, 450000, China.
authors.forename: Yao
authors.initials: Y
authors.lastname: Yao
authors.affiliation: Synthetic and Functional Biomolecules Center, College of Chemistry and Molecular Engineering, Peking University, Beijing, China.
authors.forename: Jian
authors.initials: J
authors.lastname: Lin
authors.affiliation: Synthetic and Functional Biomolecules Center, College of Chemistry and Molecular Engineering, Peking University, Beijing, China.
authors.forename: Riyong
authors.initials: R
authors.lastname: Li
authors.affiliation: Xinjiang Key Laboratory of Biological Resources and Genetic Engineering, College of Life Science and Technology, Xinjiang University, 14 Shengli Rd., Urumqi, 830046, China. Electronic address: jwli67@sina.com.
authors.forename: Jiang-Wei
authors.initials: JW
authors.lastname: Li
mesh_terms: D019843:Archaeal Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D004926:Escherichia coli / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D005293:Ferritins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D015870:Gene Expression; D006801:Humans; D010088:Oxidoreductases; D020027:Pyrococcus furiosus / Q000201:enzymology / Q000235:genetics*; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D013879:Thioredoxins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification
chemical_list: D019843:Archaeal Proteins; D011993:Recombinant Fusion Proteins; D013879:Thioredoxins; D005293:Ferritins; C454461:FTH1 protein, human; D010088:Oxidoreductases
keywords: Expression; FTH1; Ferritin; Nanocage; Peptide; Purification