Zhang Xiaorong, Zang Jiachen, Chen Hai, Zhou Kai, Zhang Tuo, Lv Chenyan, Zhao Guanghua
Beijing Advanced Innovation Center for Food Nutrition and Human Health, College of Food Science & Nutritional Engineering, China Agricultural University, Key Laboratory of Functional Dairy, Ministry of Education Beijing 100083 China
RSC Adv. 2019 Aug 9;9(43):24777-24782. doi: 10.1039/c9ra04785a. eCollection 2019 Aug 8.
Protein nanocages have been used as functional bio-templates for the synthesis or organization of nanomaterials. However, the stability of these protein nanocages is nonideal, which limits their applications. Herein, we characterized the high thermal stability of plant ferritin, soybean seed H-2 ferritin (SSFH-2), the melting point ( ) of which is 106 °C. We demonstrated that the hyperthermostability of SSFH-2 is derived from extra peptides (EP) located on its outer surface. Indeed, removal of the EP domains resulted in a dramatic decrease in to 88 °C. Similar to EP-deleted plant ferritin, human H-chain ferritin (HuHF) has a of 82 °C. Excitingly, the graft of the EP domain on the exterior surface of HuHF pronouncedly improved its to 103 °C, which represents a simple, efficient approach to the construction of protein architectures with high stability. The remarkable stability of protein nanocages will greatly facilitate their application as robust biotemplates in the field of nanoscience.
蛋白质纳米笼已被用作合成或组织纳米材料的功能性生物模板。然而，这些蛋白质纳米笼的稳定性并不理想，这限制了它们的应用。在此，我们表征了植物铁蛋白大豆种子H-2铁蛋白（SSFH-2）的高热稳定性，其熔点为106°C。我们证明，SSFH-2的超热稳定性源于位于其外表面的额外肽段（EP）。事实上，去除EP结构域导致熔点急剧下降至88°C。与缺失EP的植物铁蛋白类似，人H链铁蛋白（HuHF）的熔点为82°C。令人兴奋的是，将EP结构域嫁接到HuHF的外表面显著提高了其熔点至103°C，这代表了一种构建具有高稳定性蛋白质结构的简单、有效方法。蛋白质纳米笼的卓越稳定性将极大地促进它们作为稳健生物模板在纳米科学领域的应用。
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