纳米笼
铁蛋白
酶
化学
蛋白质水解
融合蛋白
荧光
蛋白质工程
绿色荧光蛋白
生物物理学
纳米颗粒
生物化学
纳米技术
催化作用
材料科学
生物
物理
量子力学
基因
重组DNA
作者
Stephan Tetter,Donald Hilvert
标识
DOI:10.1002/ange.201708530
摘要
Abstract Ferritins, conserved across all kingdoms of life, are protein nanocages that evolved to mineralize iron. The last several decades have shown that these cages have considerable technological and medical potential owing to their stability and tolerance to modification, as well as their ability to template nanoparticle synthesis and incorporate small molecules. Here we show that it is possible to encapsulate proteins in a ferritin cage by exploiting electrostatic interactions with its negatively charged interior. Positively supercharged green fluorescent protein is efficiently taken up by Archaeoglobus fulgidus ferritin in a tunable fashion. Moreover, several enzymes were readily incorporated when genetically tethered to this fluorescent protein. These fusion proteins retained high catalytic activity and showed increased tolerance to proteolysis and heat. Equipping ferritins with enzymatic activity paves the way for many new nanotechnological and pharmacological applications.
科研通智能强力驱动
Strongly Powered by AbleSci AI