Professor Mehdi Mobli

Professorial Research Fellow

Australian Institute for Bioengineering and Nanotechnology
m.mobli@uq.edu.au
+61 7 334 60352

Overview

Professor Mobli is a structural biologist and a group leader at the University of Queensland's Australian Institute for Bioengineering and Nanotechnology (AIBN). He is well known internationally for his contributions to the basic theory of multidimensional nuclear magnetic resonance and its applications to resolving the molecular structure of peptides and proteins, as well as studying their physiochemical properties and function. Mehdi's contributions to the field has been recognised by being appointed an Executive Editor of the AMPERE society's journal "Magnetic Resonance", and to the advisory board of the international Biological Magnetic Resonance Data Bank (BMRB) as well as serving on the board of directors of the Australia and New Zealand Society for Magnetic Resonance (ANZMAG). He is a former ARC Future Fellow and recipient of the ASBMB MERCK medal, the Australia Peptide Society's Tregear Award, the ANZMAG Sir Paul Callaghan medal and the Lorne Proteins Young Investigator Award (now Robin Anders Award).

Prof. Mobli's research group focuses on characterising the structure and function of receptors involved in neuronal signalling, with a particular focus on developing new approaches for the discovery and characterisation of modulators of these receptors through innovations in bioinformatics, biochemistry and and biophysics. This work has led to publication of more than 100 research articles attracting over 6,000 citations.

Research Interests

  • Structure, function and dynamics of biomolecules studied in solution by NMR spectroscopy
    Nuclear magnetic resonance is one of the most powerful atomic resolution techniques for probing the physicochemical properties of molecules. In biophysics and particularly in protein research NMR can uniquely be used to determine both high-resolution structures and conformational dynamics of proteins in their natural solution state environment. NMR can further be used to provide functional data and is routinely used as a screening tool to provide input to structure based drug design studies. The properties that make NMR such a versatile technique also require technical expertise in data acquisition, analysis and interpretation. Dr Mobli's research is focused on the application of NMR spectroscopy in molecular biology, with the aim of increasing the utility of the technique itself through automation and also to expand its current applications. His group are working on diverse biological problems including understanding the structure of disulfide stabilised peptides, how voltage-gated ion channels are modulated by natural and synthetic ligands and the mechanism of bacterial transcription pausing. All of these projects are being pursued with the ultimate goal of developing novel drugs and diagnostic tools.

Research Impacts

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. Prof. Mobli's research 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. His group has directly contributed over 40 high-resolution structures of constrained peptides to the PDB, including arguably the highest resolution solution structure of a disulfide-constrained peptide to date (6URP). Detailed dynamic and functional studies 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.

Qualifications

  • Doctor of Philosophy, University of Liverpool

Publications

  • Rahaman, Md. Habibur, Thygesen, Sara J., Maxwell, Michael J., Kim, Hyoyoung, Mudai, Prerna, Nanson, Jeffrey D., Jia, Xinying, Vajjhala, Parimala R., Hedger, Andrew, Vetter, Irina, Haselhorst, Thomas, Robertson, Avril A. B., Dymock, Brian, Ve, Thomas, Mobli, Mehdi, Stacey, Katryn J. and Kobe, Bostjan (2024). o-Vanillin binds covalently to MAL/TIRAP Lys-210 but independently inhibits TLR2. Journal of Enzyme Inhibition and Medicinal Chemistry, 39 (1) 2313055, 2313055. doi: 10.1080/14756366.2024.2313055

  • Ramanujam, Venkatraman, Crawford, Theo, Cristofori-Armstrong, Ben, Deuis, Jennifer, Jia, Xinying, Maxwell, Michael, Jami, Sina, Ma, Linlin, Vetter, Irina and Mobli, Mehdi (2024). Structural basis of the bivalency of the TRPV1 agonist DkTx. Angewandte Chemie International Edition, 63 (3) e202314621, 1-8. doi: 10.1002/anie.202314621

  • Ramanujam, Venkatraman, Crawford, Theo, Cristofori‐Armstrong, Ben, Deuis, Jennifer R., Jia, Xinying, Maxwell, Michael J., Jami, Sina, Ma, Linlin, Vetter, Irina and Mobli, Mehdi (2024). Structural basis of the bivalency of the TRPV1 agonist DkTx. Angewandte Chemie, 136 (3), 1-8. doi: 10.1002/ange.202314621

View all Publications

Grants

View all Grants

Supervision

  • Doctor Philosophy

  • Doctor Philosophy

  • Doctor Philosophy

View all Supervision

Publications

Book

Book Chapter

  • Miljenovic, Tomas Marko, Jia, Xinying and Mobli, Mehdi (2018). Nonuniform sampling in biomolecular NMR. Modern magnetic resonance. (pp. 2035-2054) edited by Graham A. Webb. Cham, Switzerland: Springer International Publishing. doi: 10.1007/978-3-319-28388-3_118

  • Mobli, Mehdi and Hoch, Jeffrey C. (2017). Fast NMR data acquisition: beyond the Fourier transform: Preface. Fast NMR data acquisition: beyond the Fourier transform. (pp. VIII-X) edited by Mehdi Mobli and Jeffrey C. Hoch. Cambridge, United Kingdom: Royal Society of Chemistry.

  • Mobli, Mehdi, Stern, Alan S. and Hoch, Jeffrey C. (2017). Maximum entropy reconstruction. Fast NMR data acquisition: beyond the Fourier transform. (pp. 252-266) edited by Mehdi Mobli and Jeffrey C. Hoch. Cambridge, United Kingdom: Royal Society of Chemistry.

  • Fry, B. G., Undheim, E. A. B., Jackson, T. N. W., Georgieva, D., Vetter, I., Calvete, J. J., Schieb, H., Cribb, B. W., Yang, D. C., Daly, N. L., Manchadi, M. L. Roy, Gutierrez, J. M., Roelants, K., Lomonte, B., Nicholson, G. M., Dziemborowicz, S., Lavergne, V., Ragnarsson, L., Rash, L. D., Mobli, M., Hodgson, W. C., Casewell, N. R., Nouwens, A., Wagstaff, S. C., Ali, S. A., Whitehead, D. L., Herzig, V., Monagle, P., Kurniawan, N. D. ... Sunagar, K. (2015). Research methods. Venomous reptiles and their toxins: evolution, pathophysiology and biodiscovery. (pp. 153-214) New York, NY, United States: Oxford University Press.

  • Lavergne, Vincent, Alewood, Paul F., Mobli, Mehdi and King, Glenn F. (2015). The Structural Universe of Disulfide-Rich Venom Peptides. Venoms to Drugs : Venom as a Source for the Development of Human Therapeutics. (pp. 37-79) edited by King, Glenn F.. London, United Kingdom: Royal Society of Chemistry. doi: 10.1039/9781849737876-00037

  • Maciejewski, Mark W., Mobli, Mehdi, Schuyler, Adam D., Stern, Alan S. and Hoch, Jeffrey C. (2012). Data sampling in multidimensional NMR: fundamentals and strategies. Novel sampling approaches in higher dimensional NMR. (pp. 49-77) edited by Martin Billeter and Vladislav Orekhov. Heidelberg, Germany: Springer. doi: 10.1007/128_2011_185

  • Hoch, Jeffrey C., Maciejewski, Mark W., Mobli, Mehdi, Schyler, Adam D. and Stern, Alan S. (2012). Nonuniform sampling in multidimensional NMR. EMagRes. (pp. 1-2) London, United Kingdom: John Wiley & Sons. doi: 10.1002/9780470034590.emrstm1239

  • Mobli, Mehdi, Hoch, Jeffrey C. and King, Glenn F. (2011). Fast acquisition methods in multidimensional NMR. Biomolecular NMR spectroscopy. (pp. 305-337) edited by Andrew J. Dingley and Steven M. Pascal. Amsterdam , Netherlands: IOS Press. doi: 10.3233/978-1-60750-695-9-305

  • Hoch, Jeffrey C., Stern, Alan S. and Mobli, Mehdi (2011). Maximum Entropy Reconstruction. eMagRes. (pp. 1-6) United Kingdom: John Wiley and Sons. doi: 10.1002/9780470034590.emrstm0299.pub2

  • King, Glenn F and Mehdi Mobli (2010). Determination of peptide and protein structures using NMR Spectroscopy. Comprehensive natural products II: Chemistry and biology. (pp. 280-325) edited by Lewis Mander and Hung-Wen Liu. Oxford, England: Elsevier Science & Technology Books. doi: 10.1016/B978-008045382-8.00653-5

  • Hoch, Jeffrey C. and Mobli, Mehdi (2009). Maximum Entropy: Multidimensional Methods. EMagRes. (pp. 1-8) United Kingdom: John Wiley & Sons. doi: 10.1002/9780470034590.emrstm1158

Journal Article

Conference Publication

Other Outputs

Grants (Administered at UQ)

PhD and MPhil Supervision

Current Supervision

  • Doctor Philosophy — Principal Advisor

  • Doctor Philosophy — Principal Advisor

  • Doctor Philosophy — Principal Advisor

  • Doctor Philosophy — Principal Advisor

  • Doctor Philosophy — Principal Advisor

    Other advisors:

  • Doctor Philosophy — Principal Advisor

  • Doctor Philosophy — Principal Advisor

  • Doctor Philosophy — Principal Advisor

    Other advisors:

  • Doctor Philosophy — Associate Advisor

  • Doctor Philosophy — Associate Advisor

  • Doctor Philosophy — Associate Advisor

  • Doctor Philosophy — Associate Advisor

    Other advisors:

Completed Supervision