Protein Cages: From Fundamentals to Advanced Applications

Abstract

Proteins that self-assemble into polyhedral shell-like structures are useful molecular containers both in nature and in the laboratory. Here we review efforts to repurpose diverse protein cages, including viral capsids, ferritins, bacterial microcompartments, and designed capsules, as vaccines, drug delivery vehicles, targeted imaging agents, nanoreactors, templates for controlled materials synthesis, building blocks for higher-order architectures, and more. A deep understanding of the principles underlying the construction, function, and evolution of natural systems has been key to tailoring selective cargo encapsulation and interactions with both biological systems and synthetic materials through protein engineering and directed evolution. The ability to adapt and design increasingly sophisticated capsid structures and functions stands to benefit the fields of catalysis, materials science, and medicine.

Protein–Calixarene Complexation: From Recognition to Assembly

“…Different preparation strategies are in development, 77 including designed protein assembly 78 and the repurposing of natural protein cages. 79 Macrocycle-mediated protein assembly confers advantages such as ease of fabrication and enhanced functionality via host–guest chemistry. 3 , 4 …”

Quantitative electrostatic force tomography for virus capsids in interaction with an approaching nanoscale probe

“…In particular, the interactions at the atomistic and molecular (subnanometric) resolutions are of predominant interest in proteinaceous capsids, membranes and whole viruses. [1][2][3][4][5][6][7][8] For a few decades, the physical virology community has employed diverse experimental techniques, like force microscopy, to learn more about the mechanical and electrostatic properties of biomacromolecular systems. [9][10][11][12][13][14][15][16][17][18][19] However, the amount of viruses that are electrostatically characterized at the nanoscale (i.e.…”

Engineered protein nanocages for concurrent RNA and protein packagingin vivo

“…Over the past decade, protein nanocages have gained much attention for various biotechnological and biomedical applications due to their unique and desirable properties. [1][2][3] Their biological origin makes them inherently biocompatible and allows facile genetic functionalization, while their defined shell-like structure enables the creation of multifunctional and atomically defined nano-devices by modifying both their inner and outer surfaces. Further, established recombinant protein production strategies make protein-based nanostructures simple to produce, purify, and scale.…”

“…[62] A topic of particular current interest is the selective packaging and delivery of nucleic acids inside protein-based cages. [1,63] Engineering such systems has shed light on the evolution and function of viruses and allowed the creation of non-viral systems mimicking select virus characteristics. [21,[64][65][66] The ability to encapsulate nucleic acids in vivo may provide novel approaches for RNA regulation and cytosolic sampling [21] with broad implications for RNA biology.…”