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In vivo self-assembly of an intact functional cage protein: Intracellular generation of chimeric ferritins without disassembly-involved damage
Journal of Industrial and Engineering Chemistry ( IF 5.9 ) Pub Date : 2024-06-28 , DOI: 10.1016/j.jiec.2024.06.040
Koung Hee Kim , Mi-Ran Ki , Thi Khoa My Nguyen , Ki Ha Min , Seung Pil Pack

Ferritin (Fn) is an attractive nano-biomaterial with a hollow structure. Functional chimeric cage-protein Fns (chimera-Fn) can be designed by combining two different monomer subunits. However, unavoidable damage is induced by the severe disassembly conditions required for preparing the Fn monomer. Here, a biocompatible method using a designed dual-expression vector to obtain chimera-Fns without a damage-inducing process is described. Fn monomer and silica-forming peptide (Kpt)-fused Fn monomer are expressed simultaneously and assembled within host-cells to form chimera-Fn of Kpt. Characteristic analysis showed that the chimera-Fns obtained intracellularly were composed of the two monomers in a ratio of 1:1. Morphological and functional analyses determined that the intracellularly-generated chimera-Fns had more intact forms and bioactive functions compared with those produced by chemical-involved disassembly and reassembly. This is the first report about the self-assembly of chimera-Fn with intact function and hold promise in designing functional templates for various nanomaterial preparations.

中文翻译:


完整功能性笼蛋白的体内自组装:细胞内生成嵌合铁蛋白,无拆卸相关损伤



铁蛋白(Fn)是一种有吸引力的具有中空结构的纳米生物材料。功能性嵌合笼蛋白 Fns (chimera-Fn) 可以通过组合两个不同的单体亚基来设计。然而,制备 Fn 单体所需的严格分解条件会导致不可避免的损坏。在这里,描述了一种使用设计的双表达载体来获得嵌合Fns而无需损伤诱导过程的生物相容性方法。 Fn 单体和二氧化硅形成肽 (Kpt) 融合的 Fn 单体同时表达并在宿主细胞内组装,形成 Kpt 的嵌合体 Fn。特征分析表明,细胞内获得的嵌合Fns由两种单体以1:1的比例组成。形态学和功能分析确定,与化学涉及的拆卸和重组产生的嵌合体-Fns相比,细胞内产生的嵌合体-Fns具有更完整的形式和生物活性功能。这是第一份关于具有完整功能的嵌合体-Fn自组装的报告,并有望为各种纳米材料制剂设计功能模板。
更新日期:2024-06-28
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