Venoms to drugs: translating toxins into therapeutics and bioinsecticides

Professor Glenn King

We are interested in the evolution, structure, pharmacology, and potential therapeutic and agricultural applications of disulfide-stabilised peptides from the venoms of spiders, scorpions, centipedes, and other venomous animals. Our primary focus is the discovery, structure-function characterisation, and therapeutic development of venom peptides that modulate the activity of neuronal ion channels involved in pain signalling in humans. Molecules that antagonise these ion channels have the potential to be developed as analgesics. We also have a major interest in the discovery, characterisation, and development of insecticidal peptides for the control of crop and livestock pests as well as vectors of human and animal diseases. Most research projects are highly interdisciplinary and the experimental techniques employed range from molecular biology through protein chemistry to structure determination using both NMR spectroscopy and X-ray crystallography.


Research Projects

• Development of novel analgesic drugs based on spider-venom peptides


• Development of novel anti-stroke therapeutics based on spider-venom peptides


• Development of eco-friendly bioinsecticides based on spider-venom peptides


• Molecular evolution of spider and centipede venoms

Key Publications

King, G.F., and Hardy, M.C. (2012). Spider-venom peptides: structure, pharmacology, and potential for control of insect pests. Annual Review of Entomology 58: in press.

King, G.F. (2011). Venoms as a platform for human drugs: translating toxins into therapeutics. Expert Opinion on Biological Therapy 11: 1469–1484.

Saez, N.J., Mobli, M., Bieri, M., Malde, A.K., Gamsjaeger, R., Mark, A.E., Gooley, P.R., Rash, L.D., and King, G.F. (2011). A dynamic pharmacophore drives the interaction between psalmotoxin-1 and the putative drug target acid-sensing ion channel 1a. Molecular Pharmacology 80: 796–808.

Smith, J.J., Hill, J.M., Little, M.J., Nicholson, G.M., King, G.F. and Alewood, P.F. (2011) Unique scorpion toxin with a putative ancestral fold provides insight into evolution of the inhibitor cystine knot motif. Proceedings of the National Academy of Sciences USA 108: 10478–10483.

Pang, S.S., Berry, B., Chen, Z., Kjer-Nielsen, L., Perugini, M.A., King, G.F., Wang, C., Chew, S.H., La Gruta, N.L., Williams, N.K., Beddoe, T., Tiganis, T., Cowieson, N.P., Godfrey, D.I., Purcell, A.W., Wilce, M.C.J., McCluskey, J. and Rossjohn, J. (2010) The structural basis for autonomous dimerization by the pre T-cell antigen receptor. Nature 467: 844–848.

Mobli, M., Dantas de Araújo, A., Lambert, L., Pierens, G.K., Windley, M.J., Nihcolson, G.M., Alewood, P.F., and King, G.F. (2009) Direct visualization of disulfide bonds through diselenide proxies using 77Se NMR. Angewandte Chemie International Edition 48: 9312–9314.

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