About

The Peyton Lab uses combined computational and experimental approaches to investigate protein and peptide structure, dynamics and interactions with a focus on post-translational modifications, aging and amyloid diseases. Dr Peyton is also passionate about technology-embedded teaching and is researching how to enhance chemistry teaching using augmented reality.

The Peyton Lab uses experimental and computational approaches to arrive at answers regarding protein and peptide structural changes, dynamics and interactions. Our lab specialises in solid-phases peptide synthesis, biophysical characterisation and molecular dynamics simulations. A range of computational tools, such as MODELLER, Autodock, GROMACS and AMBER, are used to perform de novo and templated peptide design, docking, and simulations of protein unfolding, self-assembly, biomolecule interactions and aggregation.

Post-translational Modifications and Amyloidogenesis

The main focus of our research group is in determining conformational consequences of post-translational modifications in proteins and peptides. Our main area of study is determining if some post-translational modifications result in aggregation-prone conformations that could play a role in amyloid diseases. Our group is currently investigating amino acid isomerisation, SUMOylation, phosphorylation and ubiquitination.

Non-natural Amino Acid Propensities

Non-natural amino acids are an interesting solution to peptide drug design. Incorporating non-natural amino acids into peptides and proteins can allow control of active site conformations, alter protein folding behaviour and increase their bio-availability by reducing the susceptibility to proteolytic degradation. We are interested in studying the conformational propensities of non-natural amino acids in order to identify ways in which design of controlled conformations can be managed.  In collaboration with the Martin group a recent project is examining the conformational properties of novel non-natural amino acids.