Research

Spider silks are renowned for their outstanding mechanical properties. Some spider species produce up to seven distinct protein-based silks with different combinations of strength and extensibility for disparate biological purposes. Many of these silks remain ill-understood, providing intriguing targets for study and bio-inspired materials development.

We develop and produce recombinant spider silk proteins, applying a wide variety of biophysical and materials science techniques to study the protein pre-assembly state in fibre, film, sponge, and nanoparticle formats. A major focus of our work is developing atomic-level structural understanding of spider silks and using this to engineer silks with different functionality, including mechanical performance and biochemical features.

This video by Anupama Ghimire demonstrates our current silk fibre wet-spinning process (detailed in Simmons et. al. (2019) ACS Biomater Sci Eng).

We routinely ask and answer experimental questions using both solution- and solid-state NMR spectroscopy, including by:

• Developing and applying ¹⁹F NMR spectroscopy methods
• 3D protein and peptide structural determination
• Evaluation of intramolecular dynamics through spin relaxation
• Quantifying hydrodynamic behaviour of macromolecules and supramolecular assemblies by pulsed-field gradient diffusion NMR methods
• Characterizing changes to molecular fold, stability, and self-assembly as a function of temperature, pressure, denaturant, detergent, etc.

We have had a longstanding interest in peptide-activated G-protein coupled receptors (GPCRs).

Our work has focused on the apelin receptor (APJ) and its peptide ligands (apelin and ELABELA/apela), developing biophysical understanding of ligand-membrane interactions and key peptide features underpinning receptor recognition to inform peptide analogue design.