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首页> 外文期刊>Molecular biology reports >Cellular binding analysis of recombinant hybrid heteropolymer of camel hepcidin and human ferritin H chain. The unexpected human H-ferritin binding to J774 murine macrophage cells
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Cellular binding analysis of recombinant hybrid heteropolymer of camel hepcidin and human ferritin H chain. The unexpected human H-ferritin binding to J774 murine macrophage cells

机译：骆驼肝素和人铁蛋白H链重组杂交杂化聚合物的细胞结合分析。 意外的人H-铁蛋白与J774鼠巨噬细胞结合

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摘要

Ferritin is a molecule with enormous potentiality in biotechnology that have been already used to encapsulate molecules, as contrast in magnetic resonance imaging and to carry epitopes. We proposed to use it to carry another key protein of iron metabolism, hepcidin that is a small hormone peptide that control systemic iron homeostasis. In this work, we purified the previously produced camel hepcidin and human H-ferritin heteropolymer (HepcH-FTH) and to monitor its binding capability toward J744 cell line in presence or absence of ferric ammonium citrate. Fused camel hepcidin and human H-ferritin monomer (HepcH) as well as the assembled HepcH-FTH heteropolymer (ratio 1:5) was easily purified by a one-step purification using size exclusion chromatography. SDS-PAGE electrophoresis of HepcH, purified from soluble and insoluble fractions, showed a single band of 24 kDa with an estimated purity of at least 90%. The purification yields of HepcH from the soluble and insoluble fractions was, respectively, of about 6.80 and 2 mg/L of bacterial culture. Time curse cellular binding assays of HepcH-FTH revealed its great potential to bind the J774 cells after 15 min of incubation. Furthermore, HepcH-FTH was able to degrade ferroportin, the unique hepcidin receptor, even after 30 min of incubation with J774 cells treated with 100 mu M ferric ammonium citrate. In conclusion, we proposed ferritin as a peptide carrier to promote the association of the hybrid HepcH-FTH nanoparticle with a particular type of cell for therapeutic or diagnostic.
机译：铁蛋白是具有已经用于封装分子的生物技术潜在具有巨大潜力的分子，其在磁共振成像和携带表位中的对比度。我们建议使用它来携带铁代谢的另一个关键蛋白，是一种小型激素肽，可控制系统性铁袜。在这项工作中，我们纯化了先前产生的骆驼肝素和人H-铁蛋白杂化物（Hepch-Fth）并在存在或不存在柠檬酸铁铵的情况下监测其对J744细胞系的结合能力。通过使用尺寸排阻色谱法通过一步纯化容易纯化熔骆驼庚酰嘧啶和人H-铁蛋白单体（Hepch）以及组装的Hepch-Fth杂聚合物（比例1：5）。 Hepch的SDS-PAGE电泳，溶于溶于和不溶性级分纯化，显示出24kDa的单带，估计纯度至少为90％。来自可溶性和不溶性级分的HEPCH的纯化产率为约6.80和2mg / L的细菌培养物。 Hepch-Fth的时间静止细胞结合测定显示其在孵育15分钟后结合J774细胞的巨大潜力。此外，即使在用100μm柠檬酸铵处理的J774细胞孵育30分钟后，Hepch-Fth能够降解丁氏蛋白，独特的肝素受体。总之，我们提出了作为肽载体的铁蛋白，以促进杂交Hepch-Fth纳米颗粒与特定类型的细胞的缔合的治疗或诊断载体。

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