Engineering protein nanocages for biotechnology applications (LE BRUN_U27DTP)

Proteins that self-assemble to yield cage-like structures are of great interest due to their potential applications in biotechnology. The cellular protein ferritin, which functions to detoxify and store iron, is composed of 24 subunits, arranged in a highly symmetric fashion to form an approximately spherical protein shell surrounding a hollow centre. While evolved to store large amounts of iron as a ferric-oxy-hydroxide mineral, the ferritin protein shell can potentially accommodate a range of other molecules. The aim of this project is to use engineering biology approaches to develop bacterial and human ferritins as nanocage platforms for the encapsulation of small molecules, peptides and proteins with applications in biocatalysis and therapeutics/diagnostics. Methodologies for encapsulation will be optimised, and the ability of the nanocages to transfer substrates, electrons and protons across the protein coat investigated. Eventual targets include technologically relevant enzymes such as hydrogenase, which catalyses the reduction of protons to hydrogen gas, and the targeted delivery of molecules for therapeutic and diagnostic applications.

This multi-disciplinary protein biochemistry project, which is based in the Le Brun lab in the School of Chemistry, Pharmacy and Pharmacology at UEA, will involve protein purification, bioanalytical methods, spectroscopy, mass spectrometry and microscopy. It offers excellent training potential for the appointed student within a supportive and stimulating environment. Informal enquiries to Prof Nick Le Brun (n.le-brun@uea.ac.uk) are welcome.