Self-assembled protein nanocompartments

Innovative materials for catalysis and drug delivery
Nature is a master of self-assembly, creating nanoscale architectures that are otherwise impossible to build synthetically. In our lab, we re-engineer these natural systems to construct new catalysts and drug delivery systems.

Left: Encapsulin nanocompartments can be used to assemble nanoreactors with unique properties.

Right: Transmission electron microscopy image of highly-monodisperse encapsulin compartments.


We have several ongoing research projects that involve chemical and biological modification of encapsulins, bacterial proteins that spontaneously assemble into hollow ~30 nm compartments (see Nat. Microbiol. 2017, 2, 17029). We can create nano-sized reaction vessels and drug carriers by functionalising the interior of these compartments with synthetic proteins and small molecules.

Encapsulin nanocompartments can be self-assembled and isolated from engineered E. coli and yeast. The compartments have remarkable stability and can protect their internal cargo from degradation. As encapsulins are highly engineerable, we can scaffold multiple proteins within their interior, and conduct catalysis with encapsulated enzymes (see Nat. Commun. 2018, 9, 1131).

The future of this research is to combine synthetic chemistry with engineered encapsulins, opening up a whole new area of chemical space and functionality that cannot be achieved by genetic techniques alone.

This research involves a mix of organic chemistry, synthetic biology and protein engineering, and is conducted in collaboration with Dr Tobias Giessen (Harvard University, USA).

Yu Heng Lau

Discovery Early Career Award (DECRA) Fellow
  • School of Chemistry F11