Mobli Group

Bioactive peptides have long been recognised as important messengers in cellular communication and are integral to our understanding of basic physiological processes. Their potential as natural substrates for biological receptors has been leveraged successfully in some of the most important therapeutics of our time, such as insulin and oxytocin. In recent years, increased attention has been given to this molecular class due to the ease of generating large libraries of these peptides under selection pressure. This can yield potent drug leads through mRNA and phage display technologies. The potency and selectivity of these molecules come from their well-defined three-dimensional structures, which are often constrained by side-chain and/or backbone linkages that stabilise their 3D shape. Our group has contributed significantly to the understanding of the structure, dynamics, and function of constrained peptides.

Our basic understanding of the physicochemical properties of bioactive peptides comes from studies of their structural and chemical properties. The Mobli group uses cutting edge biophysical methods to study the structure and function of constrained peptides. Our detailed studies of the peptide structure, dynamics and and function have offered novel insights ranging from the basic chemistry of peptide side chains to the structural basis of peptide-receptor interactions and the evolution of neofunctionalisation of stable structural scaffolds.

Partner with the Mobli Group