Prof. Mobli specialises in studying the structure and function of constrained peptides and their receptors.

Prof. Mehdi Mobli (PhD, 2004) is a Professorial Research Fellow. His research is in the field of structural biology, where his research group has a particular interest in studies of disulfide-constrained peptides, including animal venom peptides, hormones and antimicrobial peptides. These molecules are studied to understand how they modulate various receptors of medical and agricultural significance, including ion-channels and enzymes. In addition, his group is also well known for technical and theoretical contributions to the field of nuclear magnetic resonance (NMR) spectroscopy. Mehdi graduated with a degree in chemical engineering from Chalmers University of Technology in Sweden. He was awarded an industry-sponsored CASE award by GlaxoSmithKline, to undertake a PhD degree at the University of Liverpool (UK). His first postdoctoral position was at the University of Connecticut School of Medicine, where he focused on improving the resolution and throughput of protein structure determination using NMR. Following a brief postdoctoral position at the University of Manchester, working on the role of dynamics in the biological function of glycans, he moved to UQ where he worked on the structural elucidation of spider venom peptides. Mehdi established his research group in 2012 through the award of an ARC Future Fellowship. He has published more than100 research articles, 13 book chapters and 2 books. He was awarded the 2013 Sir Paul Callaghan Medal of the ANZMAG Society for his contributions to the field of NMR spectroscopy and later he received the 2017 Tregear Award by the Australian Peptide Society for his work in the field of Peptide research and most recently he received the 2018 MERCK Research Medal from the Australian Society for Biochemistry and Molecular Biology for his contributions to structural biology.

Collaborations

The interdisciplinary nature of Prof. Mobli's research requires an extensive collaborative network from institutional to international colleagues. The nature of the collaborations is driven by the research question and ranges from experts in related structural biology techniques to those with relevant expertise in cellular and animal models relating to the function of the peptides studied in the group.

Funding

Prof. Mobli established his group in 2012 through an ARC Future Fellowship and a subsequent sole-investigator ARC Discovery Project, focusing on developing and applying tools for the characterisation of bioactive peptide structure and function. Since 2015, his research has attracted $9.3 million from the ARC and the NHMRC, including $3.5 million since 2019 as lead investigator.

Key Publications

Ramanujam, V., Crawford, T., Cristofori-Armstrong, B., Deuis, J.R., Jia, X., Maxwell, M.J., Jami, S., Ma, L., Vetter, I., and Mobli, M. (2024). Structural Basis of the Bivalency of the TRPV1 Agonist DkTx. Angew Chem Int Ed Engl 63, e202314621.

Maxwell, M.J., Thekkedam, C., Lamboley, C., Chin, Y.K., Crawford, T., Smith, J.J., Liu, J., Jia, X., Vetter, I., Laver, D.R., et al. (2023). A bivalent remipede toxin promotes calcium release via ryanodine receptor activation. Nat Commun 14, 1036.

Jia, X., Chin, Y.K., Zhang, A.H., Crawford, T., Zhu, Y., Fletcher, N.L., Zhou, Z., Hamilton, B.R., Stroet, M., Thurecht, K.J., et al. (2023). Self-cyclisation as a general and efficient platform for peptide and protein macrocyclisation. Commun Chem 6, 48.

Figley, M.D., Gu, W., Nanson, J.D., Shi, Y., Sasaki, Y., Cunnea, K., Malde, A.K., Jia, X., Luo, Z., Saikot, F.K., et al. (2021). SARM1 is a metabolic sensor activated by an increased NMN/NAD(+) ratio to trigger axon degeneration. Neuron 109, 1118-1136 e1111.

Elliott, A.G., Huang, J.X., Neve, S., Zuegg, J., Edwards, I.A., Cain, A.K., Boinett, C.J., Barquist, L., Lundberg, C.V., Steen, J., et al. (2020). An amphipathic peptide with antibiotic activity against multidrug-resistant Gram-negative bacteria. Nat Commun 11, 3184.

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