Recent years have witnessed the emergence of bacterial semiorganelle encapsulins as promising platforms for bio-nanotechnology. To advance the development of encapsulins as nanoplatforms, a functional and structural basis of these assemblies is required. Encapsulin from Brevibacterium linens is known to be a protein-based vessel for an enzyme cargo in its cavity, which could be replaced with a foreign cargo, resulting in a modified encapsulin. Here, we characterize the native structure of B. linens encapsulins with both native and foreign cargo using cryo-electron microscopy (cryo-EM). Furthermore, by harnessing the confined enzyme (i.e., a peroxidase), we demonstrate the functionality of the encapsulin for an in vitro surface-immobilized catalysis in a cascade pathway with an additional enzyme, glucose oxidase. We also demonstrate the in vivo functionality of the encapsulin for cellular uptake using mammalian macrophages. Unraveling both the structure and functionality of the encapsulins allows transforming biological nanocompartments into functional systems.

Mechanically interlocked molecules (MIMs) such as rotaxanes and catenanes are capable of mechanical motion on the nanoscale and are therefore promising prototypes for molecular machines in recent nanotechnology. However, most of the existing examples are isotropically distributed in solution, which prohibits concerted movement and with it the generation of macroscopic effects. Thus, arranging them in ordered arrays is of huge interest in recent research. We report the deposition of quite densely packed multilayers of tetralactam macrocycles on gold surfaces by metal-coordinated layer-by-layer selfassembly. Linear dichroism effects in angle-resolved NEXAFS spectra indicate a preferential orientation of the macrocycles. The sequence of the metal ions can be programmed by the use of different transition metal ions at each deposition step. Additionally, reversible on-surface pseudorotaxane formation was successfully realized by repeated uptake and release of axle molecules inside the macrocycles cavities.

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Gold nanoparticles have recently gained attention as heterogeneous catalysts in a variety of industrially relevant processes. The catalytic activity of the particles is directly related to the available surface area, which increases with decreasing particle size. However, their stability in solution decreases along with the size, and surface modifications have to be carried out to enable efficient catalysis also for elongated reaction times. To prolong catalyst lifetime and to study the substrate selectivity, we encapsulated colloidal gold nanoparticles in cowpea chlorotic mottle virus cages and catalyzed the reduction of nitroarenes with different substituents. The reduction mechanism has been investigated carefully, revealing the reduction sequence nitro → hydroxylamine → amine to take place. The reduction rate is slowed by the introduction of the diffusion barrier imposed by the virus cage, and a nonconventional relation between electronic effects and reduction rate constants is reported that originates from the limited pore sizes and charged exterior/interior of the virus cage. Finally, a significantly increased stability of the hybrid nanoreactors and their recyclability are demonstrated.

Abundant and highly diverse, viruses offer new scaffolds in nanotechnology for the encapsulation, organization, or even synthesis of novel materials. In this work the coat protein of the cowpea chlorotic mottle virus (CCMV) is used to encapsulate gold nanoparticles with different sizes and stabilizing ligands yielding stable particles in buffered solutions at neutral pH. The sizes of the virus-like particles correspond to T = 1, 2, and 3 Caspar-Klug icosahedral triangulation numbers. We developed a simple one-step process enabling the encapsulation of commercially available gold nanoparticles without prior modification with up to 97% efficiency. The encapsulation efficiency is further increased using bis-p-(sufonatophenyl)phenyl phosphine surfactants up to 99%. Our work provides a simplified procedure for the preparation of metallic particles stabilized in CCMV protein cages. The presented results are expected to enable the preparation of a variety of similar virus-based colloids for current focus areas.