Current Projects

Compounds from animal venoms are invaluable research tools, important drug leads and drugs, and have elucidated unknown signalling pathways important in health and disease. Past discoveries in venom biomedical research pale in comparison to future prospects. Our research has been at the forefront of developing and applying novel computational and experimental tools to accelerate the discovery and functional characterization of venom compounds and elucidate their unique modus operandi.

Venom Discovery

We use a combination of transcriptomics, proteomics, and novel software tools to discover bioactive peptides from large libraries of venomous marine snails. Our current focus is on peptides that share structural and functional similarity to human hormones and signaling peptides. We hypothesize that these provide the fastest track from basic research to therapeutic development and application.

Venom Insulins

Following our discovery of the first insulin ever described from an animal venom we showed that venom insulins are widely distributed in marine cone snails, track prey taxa, and utilize unique ways to activate the human insulin receptor. We are currently exploring the evolution of these venom insulins and utilize structure-function studies to develop new, venom-inspired drug leads for diabetes.

Venom GPCR ligands

Humans express >800 G-protein coupled receptors (GPCRs) that are involved in the regulation of key physiological processes. Despite the high therapeutic potential of venom peptides little work has been done to discover and develop new venom-derived GPCR ligands. We have discovered several venom peptides that specifically activate GPCRs implicated in disease and are currently exploring the therapeutic potential of these peptides while also aiming to discover additional GPCR ligands.

Venom Production

Guided by our research on biosynthetic venom enzymes we are developing novel expression systems to ease the production of difficult-to-make peptides, including insulins and other peptides containing multiple disulfide bonds.

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