A Structure-Based Assembly Screen of Protein Cage Libraries in Living Cells: Experimentally Repacking a Protein-Protein Interface To Recover Cage Formation in an Assembly-Frustrated Mutant.

Cage proteins, which assemble into often highly symmetric hollow nanoscale capsules, have great potential in applications as far reaching as drug delivery, hybrid nanomaterial engineering, and catalysis. In addition, they are promising model systems for understanding how cellular nanostructures are constructed through protein-protein interactions, and they are beginning to be used as scaffolds for synthetic biology approaches. Recently, there has been renewed interest in the engineering of protein cages, and in support of these strategies, we have recently described a fluorescence-based assay for protein cage assembly that is specific for certain oligomerization states and symmetry-related protein-protein interfaces.

Influence of dopant substitution mechanism on catalytic properties within hierarchical architectures.

A range of hierarchically porous (HP) AlPO-5 catalysts, with isomorphously substituted transition metal ions, have been synthesized using an organosilane as a soft template. By employing a range of structural and spectroscopic characterization protocols, the properties of the dopant-substituted species within the HP architectures have been carefully evaluated. The resulting nature of the active site is shown to have a direct impact on the ensuing catalytic properties in the liquid-phase Beckmann rearrangement of cyclic ketones.

Predictive design of engineered multifunctional solid catalysts.

The ability to devise and design multifunctional active sites at the nanoscale, by drawing on the intricate ability of enzymes to evolve single-sites with distinctive catalytic function, has prompted complimentary and concordant developments in the field of catalyst design and in situ operando spectroscopy. Innovations in design-application approach have led to a more fundamental understanding of the nature of the active site and its mechanistic influence at a molecular level, that have enabled robust structure-property correlations to be established, which has facilitated the dextrous manipulation and predictive design of redox and solid-acid sites for industrially-significant, sustainable catalytic transformations.

Detection of specific protein-protein interactions in nanocages by engineering bipartite FlAsH binding sites.

Proteins that form cage-like structures have been of much recent cross-disciplinary interest due to their application to bioconjugate and materials chemistry, their biological functions spanning multiple essential cellular processes, and their complex structure, often defined by highly symmetric protein–protein interactions. Thus, establishing the fundamentals of their formation, through detecting and quantifying important protein–protein interactions, could be crucial to understanding essential cellular machinery, and for further development of protein-based technologies. Herein we describe a method to monitor the assembly of protein cages by detecting specific, oligomerization state dependent, protein–protein interactions.