Themed collection Materials, Physical and Biological Chemistry of Protein Cages

The properties of biocatalysis can be tuned by encapsulation of enzymes inside protein cages, which alters enzyme behaviors, substrate access and product release, and efficiency of cascade reactions.

Virus-like particles (VLPs) are self-assembled supramolecular structures in nature for compartmentalization. We summarize the current progress of protein cage nanoreactors spanning multilength scales, and highlight the emerging field of VLP based nanoreactors for biomedical applications.

There are many native and engineered capsid-forming proteins which can self-assemble into different non-canonical structures. In this review, we categorise examples of structural polymorphism by their method of formation.

All protein prokaryotic organelle in bio-material science applications.

Encapsulins are protein compartments that encapsulate cargo proteins via specific peptide targeting motifs. Fusion of these motifs to non-native cargo proteins allows the facile engineering of rationally designed nano-compartmentalization systems.

Overview of ferritin nanocage and ferritin nanozyme. The ferritin nanocages hold different modified interfaces of protein structure (upper). Ferritin nanozymes show various enzyme-like activities for different biomedical applications (bottom).

Changing the symmetry of the constituent ring-shaped building block of an artificial cage.

This study provides proof of charge complementarity-based inclusion complex formation between an engineered protein nanocage and an otherwise degradation-prone cargo protein in live bacterial cells.

Protein-based adsorber materials with defined morphology for the removal of uremic toxins.

Three-dimensional ferritin nanocage superlattices can serve as a two-compartment system for the hierarchical encapsulation and release of two different cargoes in a spatiotemporally controlled manner.

Highly ordered anisotropic assemblies of toroidal peroxiredoxin protein cage are reported by the sequential and orthogonal input of pH and chemical stimuli.

A dopamine based macromolecular glue is used to facilitate the construction of hybrid nanomaterials that are coated with virus capsid proteins, with the aim to improve stability, biocompatibility, and function.

Protein vesicle self-assembly and size can be tuned by manipulating the amino acid sequence and length of elastin like polypeptide.

The research described here looks at the development of virus-like particles (VLPs) derived from bacteriophage HK97 as versatile scaffolds for bionanomaterials construction.

Tumor-specific drug-delivering nanocarriers could be a promising modality for next-generation tumor therapy.

Qβ VLP simplified assembly approach uses the positively charged Rev tag to interact electrostatically with the negatively charged RNAs. This system exploits the known hairpins produced in the coat protein sequence to template the assembly of the full viral capsid.

Glucose oxidase and Fe₃O₄ nanoparticles were successfully loaded inside regenerated silk fibroin/zein nanospheres to obtain composite nanospheres, which have significant potential for combining starvation and chemodynamic therapy.

A modular hepatitis B virus-like particle delivery platform enables enhanced uptake and toxicity in cancer cells.

By incorporating [NiFe]-hydrogenases into a proteinaceous carboxysome shell, we generate a novel biocatalyst that has improved production of clean hydrogen, oxygen tolerance, and thermostability, highlighting its great potential in biotechnological applications.

Immunological problems have prevented applications of Virus like particles (VLPs). Here, we show that using immune-orthogonal VLPs sequentially and modifying of major immune region can circumvent immune responses after repeated administration.

We developed a multi-therapeutic organoplatinum-based drug (HFn-PtM) with good water solubility and active targeting via capturing metallacycles into the cavity of human heavy chain ferritin nanocages, which exhibited excellent anti-tumor efficiency.

Encapsulation of anti-miR-181a oligonucleotide into plant virus cowpea chlorotic mottle virus (CCMV) improves the stability of both RNA oligonucleotides. Knockdown efficacy was significantly improved with CCMV encapsulation compared to non-encapsulated counterpart.