Angewandte Chemie - International Edition
Angewandte Chemie - International Edition
4 years ago

Enzyme Encapsulation by a Ferritin Cage

Enzyme Encapsulation by a Ferritin Cage
Donald Hilvert, Stephan Tetter
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. The caged bird sings: The natural ferritin nanocage from Archaeoglobus fulgidus can encapsulate positively charged proteins (green) within its lumenal cavity through electrostatic interactions. Enzymes (gray) attached to such charged guests retain their activity [substrate (S)product (P)], thus equipping the ferritin cages with new catalytic functions and opening new avenues for their use in nanotechnology and pharmacology.

Publisher URL: http://onlinelibrary.wiley.com/resolve/doi

DOI: 10.1002/anie.201708530

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