Confining functional materials in protein based assemblies.
Amongst the toolbox of available building blocks in Nature, viruses and virus‑like particles (VLPs) have emerged as promising candidates for applications in nanotechnology. The shell of virus‑like particles is typically composed of multiple copies of identical virus coat proteins and their self‑assembly is often induced by electrostatic interactions between the virus coat protein and its molecular cargo. This reversible assembly can be used to introduce a variety of (functional) materials inside VLPs, while the symmetrical ordering of the proteins in the shell allows for the precise positioning of chemical entities.
Here, the interplay between the self‑assembly of Cowpea Chlorotic Mottle Virus (CCMV) coat proteins with functional templates will be reported. Specifically, the encapsulation of a two-component enzyme pathway in CCMV is described as a mimic of protein organelles that are recently isolated from bacteria. The encapsulation technology is described together with kinetic studies to investigate the influence of molecular confinement on enzyme efficiency. These studies confirm that bringing substrates and enzymes together in nano-sized reactors enhances the reaction rates in a comparable way to natural organelles.