Bugs and drugs

“Spider venoms are predicted to contain more than 10 million different bioactive peptides. Venoms have evolved to target the nervous systems of their prey, and neurotoxic venoms are also highly targeted within the human body, which makes them excellent drug candidates,” said Group Leader Glenn King.

“We have discovered molecules within venom that modulate ion channels. A very promising discovery that may be effective against epilepsy is entering clinical trials soon.”

The King Group have also applied their expertise in venom derived peptide chemistry to create an eco-friendly bio-insecticide. It was a significant discovery that charted new territory in the field. The resulting product will be on the market in 2017.

“We have developed a discovery pipeline that allows us to obtain venom peptide structures and structure-activity relationship data at an unprecedented rate,” said Professor King.

The Institute for Molecular Bioscience is the leading institute for venom-based drug discovery in the world. It has the biggest collection of venoms, with over 600 in the library.

Coming soon.

Research title: Bugs and drugs

Summary of research interests: Animal venoms are increasingly being used in drug discovery efforts as they constitute a vast and largely untapped source of pharmacologically active molecules. Spiders are by far the most successful group of venomous animals and their venoms are predicted to contain more than 10 million different bioactive peptides. Our group is exploring spider venoms as a source of novel peptides to provide leads for the development of new drugs and insecticides. As a major part of this initiative, we have developed a discovery pipeline that allows venom peptide structures and structure-activity relationship data to be obtained at an unprecedented rate.

Traineeships, honours and PhD projects include

• Discovery and characterisation of venom peptides targeted at ion channels involved in sensing or transmission of pain
• Discovery and characterisation of novel insecticidal and nematicidal compounds
• Structural characterisation of the interaction between venom peptides and their ion channel targets
• Examination of the genetic basis underlying the remarkable diversity and evolution of venom peptides.

Contact: Professor Glenn King

+61 7 3346 2025
glenn.king@imb.uq.edu.au

Find out more about Research Training at IMB:

• Spider-venom peptides: structure, pharmacology, and potential for control of insect pests

  King, Glenn F. and Hardy, Margaret C. (2013) Spider-venom peptides: structure, pharmacology, and potential for control of insect pests. Annual Review of Entomology, 58 475-496. doi:10.1146/annurev-ento-120811-153650

• Venoms as a platform for human drugs: Translating toxins into therapeutics

  King, Glenn F. (2011) Venoms as a platform for human drugs: Translating toxins into therapeutics. Expert Opinion on Biological Therapy, 11 11: 1469-1484. doi:10.1517/14712598.2011.621940

• Unique scorpion toxin with a putative ancestral fold provides insight into evolution of the inhibitor cystine knot motif

  Smith, Jennifer J., Hill, Justine M., Little, Michelle J., Nicholson, Graham M., King, Glenn F. and Alewood, Paul 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 of the United States of America, 108 26: 10478-10483. doi:10.1073/pnas.1103501108

• Phox homology band 4.1/ezrin/radixin/moesin-like proteins function as molecular scaffolds that interact with cargo receptors and Ras GTPases

  Ghai, Rajesh, Mobli, Mehdi, Norwood, Suzanne J., Bugarcic, Andrea, Teasdale, Rohan D., King, Glenn F. and Collins, Brett M. (2011) Phox homology band 4.1/ezrin/radixin/moesin-like proteins function as molecular scaffolds that interact with cargo receptors and Ras GTPases. Proceedings of the National Academy of Sciences of the United States of America, 108 19: 7763-7768. doi:10.1073/pnas.1017110108

• The structural basis for autonomous dimerization of the pre-T-cell antigen receptor

  Pang, Siew Siew, Berry, Richard, Chen, Zhenjun, Kjer-Nielsen, Lars, Perugini, Matthew A., King, Glenn F., Wang, Christina, Chew, Sock Hui, La Gruta, Nicole L., Williams, Neil K., Beddoe, Travis, Tiganis, Tony, Cowieson, Nathan P., Godfrey, Dale I., Purcell, Anthony W., Wilce, Matthew C. J., McCluskey, James and Rossjohn, Jamie (2010) The structural basis for autonomous dimerization of the pre-T-cell antigen receptor. Nature, 467 7317: 844-848. doi:10.1038/nature09448

• Direct Visualization of Disulfide Bonds through Diselenide Proxies Using Se-77 NMR Spectroscopy

  Mobli, M., Dantas de Araujo, A., Lambert, L. K., Pierens, G. K., Windley, M. J., Nicholson, G. M., Alewood, P. F. and King, G. E. (2009) Direct Visualization of Disulfide Bonds through Diselenide Proxies Using Se-77 NMR Spectroscopy.Angewandte Chemie International Edition, 48 49: 9312-9314. doi:10.1002/anie.200905206

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