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Heavy metal detoxification by recombinant ferritin from Apostichopus japonicus

机译：刺五加重组铁蛋白对重金属的解毒作用

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Ferritin is a bionanomaterial that is widely applied in magnetic resonance imaging, drug delivery systems, biocompatible fluorescence, neutron-capture therapy and electrochemical markers. Ferritin also has great potential for use in environmental detection and heavy metal removal due to its hollow cage sequestration and maintenance of iron in a nontoxic and bio-available form. In this study, the heavy metal binding activity of ferritin from Apostichopus japonicus (AjFER) was elucidated using scanning electron microscopy (SEM). It was observed that ferritin aggregation morphology changed dramatically upon exposure to five metals. The reaction systems formed ferritin-Cd, ferritin-As, ferritin-Hg, ferritin-Pb, and ferritin-Cr aggregations. The aggregations of horse spleen ferritin (HSF) and AjFER are relatively unified rules. The enrichment capacity of ferritin was further analyzed using Inductively Coupled Plasma Mass spectrometry. The contents of Cd2+, Hg2+, Cr3+, Pb2+, and As3+ enriched by recombinant AjFER were higher than that for the standard HSF in ordinary groups. Moreover, the concentration levels of enriched heavy metal ions in groups treated with phosphate were higher than those in ordinary dialysis control AjFER groups. The conformation stability of AjFER binding to different heavy metal ions was determined using Circular Dichroism (CD) spectroscopy, which revealed that the second structure of Mn+-ferritin has relative stability. The affinity of ferritin for metal ions was determined using Isothermal Titration Calorimetry (ITC), and the order of binding constant was Pb-Fer > Hg-Fer > Cd-Fer > As-Fer > Cr-Fer. The ion channel was measured using site-directed mutagenesis, which revealed that heavy metal ions primarily enter the protein cage via a three-fold channel and that the ferroxidase center may be one of the key sites for metal ion diffusion into the interior of the protein shell.
机译：铁蛋白是一种生物纳米材料，已广泛应用于磁共振成像，药物输送系统，生物相容性荧光，中子捕获疗法和电化学标记物。铁蛋白由于其中空的笼形螯合和以无毒且可生物利用的形式保持铁，在环境检测和重金属去除方面也具有巨大潜力。在这项研究中，使用扫描电子显微镜（SEM）阐明了日本刺槐（AjFER）中铁蛋白的重金属结合活性。观察到铁蛋白聚集形态在暴露于五种金属时发生了巨大变化。反应系统形成铁蛋白-镉，铁蛋白-As，铁蛋白-Hg，铁蛋白-Pb和铁蛋白-Cr聚集体。马脾铁蛋白（HSF）和AjFER的聚集是相对统一的规则。使用电感耦合等离子体质谱法进一步分析铁蛋白的富集能力。 Cd 2 + ，Hg 2 + ，Cr 3 + ，Pb 2 + 和As 3 + 高于普通人群中的标准HSF。而且，用磷酸盐处理的组中富集重金属离子的浓度水平高于普通透析对照AjFER组。利用圆二色光谱法测定了AjFER与不同重金属离子结合的构象稳定性，揭示了M n + 的第二结构。小铁蛋白具有相对的稳定性。铁蛋白对金属离子的亲和力用等温滴定热法（ITC）测定，结合常数的顺序为Pb-Fer> Hg-Fer> Cd-Fer> As-Fer> Cr-Fer。使用定点诱变法测量离子通道，结果表明重金属离子主要通过三倍通道进入蛋白笼，并且亚铁氧化酶中心可能是金属离子的关键位点之一扩散到蛋白质壳内部。

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