Professor Mehdi Mobli
Professor

Mehdi Mobli

Email: 
Phone: 
+61 7 334 60352

Background

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.

Availability

Professor Mehdi Mobli is:
Available for supervision
Media expert

Fields of research

Analytical biochemistry Analytical chemistry Bioinformatics and computational biology Biological Sciences Biomaterials Biomedical engineering Biomolecular modelling and design Characterisation of biological macromolecules Chemical Sciences Cheminformatics and quantitative structure-activity relationships Engineering Enzymes Information and Computing Sciences Macromolecular and materials chemistry Mathematical Sciences Medicinal and biomolecular chemistry Molecular medicine Numerical analysis Numerical and computational mathematics Optical properties of materials Organic chemistry Physical chemistry Physical organic chemistry Proteins and peptides Receptors and membrane biology Solution chemistry Structural biology (incl. macromolecular modelling) Theory of computation

Qualifications

  • Doctor of Philosophy, University of Liverpool

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.

Search Professor Mehdi Mobli’s works on UQ eSpace

146 works between 2003 and 2024
All (146) Journal Article (123) Book Chapter (11) Conference Publication (8) Book (3) Other Outputs (1)

41 - 60 of 146 works

2018

Book Chapter

Nonuniform sampling in biomolecular NMR

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

Nonuniform sampling in biomolecular NMR

2017

Journal Article

Solution structure of the TLR adaptor MAL/TIRAP reveals an intact BB loop and supports MAL Cys91 glutathionylation for signaling

Hughes, Mark M., Lavrencic, Peter, Coll, Rebecca C., Ve, Thomas, Ryan, Dylan G., Williams, Niamh C., Menon, Deepthi, Mansell, Ashley, Board, Philip G., Mobli, Mehdi, Kobe, Bostjan and O'Neill, Luke A. J. (2017). Solution structure of the TLR adaptor MAL/TIRAP reveals an intact BB loop and supports MAL Cys91 glutathionylation for signaling. Proceedings of the National Academy of Sciences, 114 (32), E6480-E6489. doi: 10.1073/pnas.1701868114

Solution structure of the TLR adaptor MAL/TIRAP reveals an intact BB loop and supports MAL Cys91 glutathionylation for signaling

2017

Journal Article

Structural basis of TIR-domain-assembly formation in MAL- and MyD88-dependent TLR4 signaling

Ve, Thomas, Vajjhala, Parimala, Hedger, Andrew, Croll, Tristan, DiMaio, Frank, Horsefield, Shane, Yu, Xiong, Lavrencic, Peter, Hassan, Zahid, Morgan, Garry P., Mansell, Ashley, Mobli, Mehdi, O'Carroll, Ailis, Chauvin, Brieuc, Gambin, Yann, Sierecki, Emma, Landsberg, Michael J., Stacey, Katryn, Egelman, Edward H. and Kobe, Bostjan (2017). Structural basis of TIR-domain-assembly formation in MAL- and MyD88-dependent TLR4 signaling. Nature Structural and Molecular Biology, 24 (9), 743-751. doi: 10.1038/nsmb.3444

Structural basis of TIR-domain-assembly formation in MAL- and MyD88-dependent TLR4 signaling

2017

Journal Article

Two proteins for the price of one: structural studies of the dual-destiny protein preproalbumin with sunflower trypsin inhibitor-1

Franke, Bastian, James, Amy M., Mobli, Mehdi, Colgrave, Michelle L., Mylne, Joshua S. and Rosengren, K. Johan (2017). Two proteins for the price of one: structural studies of the dual-destiny protein preproalbumin with sunflower trypsin inhibitor-1. The Journal of Biological Chemistry, 292 (30), 12398-12411. doi: 10.1074/jbc.M117.776955

Two proteins for the price of one: structural studies of the dual-destiny protein preproalbumin with sunflower trypsin inhibitor-1

2017

Journal Article

The tarantula toxin β/δ-TRTX-Pre1a highlights the importance of the S1-S2 voltage-sensor region for sodium channel subtype selectivity.

Wingerd, Joshua S., Mozar, Christine A., Ussing, Christine A., Murali, Swetha S., Chin, Yanni K. -Y., Cristofori-Armstrong, Ben, Durek, Thomas, Gilchrist, John, Vaughan, Christopher W., Bosmans, Frank, Adams, David J., Lewis, Richard J., Alewood, Paul F., Mobli, Mehdi, Christie, Macdonald J. and Rash, Lachlan D. (2017). The tarantula toxin β/δ-TRTX-Pre1a highlights the importance of the S1-S2 voltage-sensor region for sodium channel subtype selectivity.. Scientific Reports, 7 (1) 974, 974. doi: 10.1038/s41598-017-01129-0

The tarantula toxin β/δ-TRTX-Pre1a highlights the importance of the S1-S2 voltage-sensor region for sodium channel subtype selectivity.

2017

Journal Article

Modulation of ion channels by cysteine-rich peptides: from sequence to structure

Mobli, Mehdi, Undheim, Eivind A.B. and Rash, Lachlan D. (2017). Modulation of ion channels by cysteine-rich peptides: from sequence to structure. Advances in Pharmacology, 79, 199-223. doi: 10.1016/bs.apha.2017.03.001

Modulation of ion channels by cysteine-rich peptides: from sequence to structure

2017

Journal Article

The structure, dynamics and selectivity profile of a NaV 1.7 potency-optimised huwentoxin-IV variant

Rahnama, Sassan, Deuis, Jennifer R., Cardoso, Fernanda C., Ramanujam, Venkatraman, Lewis, Richard J., Rash, Lachlan D., King, Glenn F., Vetter, Irina and Mobli, Mehdi (2017). The structure, dynamics and selectivity profile of a NaV 1.7 potency-optimised huwentoxin-IV variant. PLoS One, 12 (3) e0173551, e0173551. doi: 10.1371/journal.pone.0173551

The structure, dynamics and selectivity profile of a NaV 1.7 potency-optimised huwentoxin-IV variant

2017

Journal Article

Potent neuroprotection after stroke afforded by a double-knot spider-venom peptide that inhibits acid-sensing ion channel 1a

Chassagnon, Irene R., McCarthy, Claudia A., Chin, Yanni K.-Y., Pineda, Sandy S., Keramidas, Angelo, Mobli, Mehdi, Pham, Vi, De Silva, T. Michael, Lynch, Joseph W., Widdop, Robert E., Rash, Lachlan D. and King, Glenn F. (2017). Potent neuroprotection after stroke afforded by a double-knot spider-venom peptide that inhibits acid-sensing ion channel 1a. Proceedings from the National Academy of Sciences of the United States of America, 114 (14), 3750-3755. doi: 10.1073/pnas.1614728114

Potent neuroprotection after stroke afforded by a double-knot spider-venom peptide that inhibits acid-sensing ion channel 1a

2017

Journal Article

A non-uniform sampling approach enables studies of dilute and unstable proteins

Miljenović, Tomas, Jia, Xinying, Lavrencic, Peter, Kobe, Bostjan and Mobli, Mehdi (2017). A non-uniform sampling approach enables studies of dilute and unstable proteins. Journal of Biomolecular NMR, 68 (2), 1-9. doi: 10.1007/s10858-017-0091-z

A non-uniform sampling approach enables studies of dilute and unstable proteins

2017

Journal Article

Synthesis of multivalent [Lys8]-oxytocin dendrimers that inhibit visceral nociceptive responses

Wan, Jingjing, Mobli, Mehdi, Brust, Andreas, Muttenthaler, Markus, Andersson, Asa, Ragnarsson, Lotten, Castro, Joel, Vetter, Irina, Huang, Johnny X., Nilsson, Mathias, Brierley, Stuart M., Cooper, Matthew A., Lewis, Richard J. and Alewood, Paul F. (2017). Synthesis of multivalent [Lys8]-oxytocin dendrimers that inhibit visceral nociceptive responses. Australian Journal of Chemistry, 70 (2), 162-171. doi: 10.1071/CH16407

Synthesis of multivalent [Lys8]-oxytocin dendrimers that inhibit visceral nociceptive responses

2017

Book Chapter

Fast NMR data acquisition: beyond the Fourier transform: Preface

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.

Fast NMR data acquisition: beyond the Fourier transform: Preface

2017

Book Chapter

Maximum entropy reconstruction

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.

Maximum entropy reconstruction

2017

Book

Fast NMR data acquisition: beyond the Fourier transform

Mehdi Mobli and Jeffrey C. Hoch eds. (2017). Fast NMR data acquisition: beyond the Fourier transform. New Developments in NMR, Cambridge, United Kingdom: Royal Society of Chemistry. doi: 10.1039/9781782628361

Fast NMR data acquisition: beyond the Fourier transform

2016

Journal Article

NaV1.7 as a pain target – from gene to pharmacology

Vetter, Irina, Deuis, Jennifer, Mueller, Alexander, Israel, Mathilde R., Hana Starobova, Zhang, Alan, Rash, Lachlan D. and Mobli, Mehdi (2016). NaV1.7 as a pain target – from gene to pharmacology. Pharmacology and Therapeutics, 172, 73-100. doi: 10.1016/j.pharmthera.2016.11.015

NaV1.7 as a pain target – from gene to pharmacology

2016

Journal Article

The CC domain structure from the wheat stem rust resistance protein Sr33 challenges paradigms for dimerization in plant NLR proteins

Casey, Lachlan W., Lavrencic, Peter, Bentham, Adam R., Cesari, Stella, Ericsson, Daniel J., Croll, Tristan, Turk, Dušan, Anderson, Peter A., Mark, Alan E., Dodds, Peter N., Mobli, Mehdi, Kobe, Bostjan and Williams, Simon J. (2016). The CC domain structure from the wheat stem rust resistance protein Sr33 challenges paradigms for dimerization in plant NLR proteins. Proceedings of the National Academy of Sciences, 113 (45), 12856-12861. doi: 10.1073/pnas.1609922113

The CC domain structure from the wheat stem rust resistance protein Sr33 challenges paradigms for dimerization in plant NLR proteins

2016

Journal Article

Determination of ligand binding modes in weak protein–ligand complexes using sparse NMR data

Mohanty, Biswaranjan, Williams, Martin L., Doak, Bradley C., Vazirani, Mansha, Ilyichova, Olga, Wang, Geqing, Bermel, Wolfgang, Simpson, Jamie S., Chalmers, David K., King, Glenn F., Mobli, Mehdi and Scanlon, Martin J. (2016). Determination of ligand binding modes in weak protein–ligand complexes using sparse NMR data. Journal of Biomolecular NMR, 66 (3), 195-208. doi: 10.1007/s10858-016-0067-4

Determination of ligand binding modes in weak protein–ligand complexes using sparse NMR data

2016

Journal Article

Molecular basis of the interaction between gating modifier spider toxins and the voltage sensor of voltage-gated ion channels

Lau, Carus H.Y., King, Glenn F and Mobli, Mehdi (2016). Molecular basis of the interaction between gating modifier spider toxins and the voltage sensor of voltage-gated ion channels. Scientific Reports, 6 (1) 34333, 34333. doi: 10.1038/srep34333

Molecular basis of the interaction between gating modifier spider toxins and the voltage sensor of voltage-gated ion channels

2016

Journal Article

Correction: Sparse sampling methods in multidimensional NMR

Mobli, Mehdi, Maciejewski, Mark W, Schuyler, Adam D, Stern, Alan S and Hoch, Jeffrey C (2016). Correction: Sparse sampling methods in multidimensional NMR. Physical Chemistry Chemical Physics, 18 (28), 19482-19482. doi: 10.1039/c6cp90157c

Correction: Sparse sampling methods in multidimensional NMR

2016

Journal Article

Toxin structures as evolutionary tools: Using conserved 3D folds to study the evolution of rapidly evolving peptides

Undheim, Eivind A., Mobli, Mehdi and King, Glenn F. (2016). Toxin structures as evolutionary tools: Using conserved 3D folds to study the evolution of rapidly evolving peptides. Bioessays, 38 (6), 539-548. doi: 10.1002/bies.201500165

Toxin structures as evolutionary tools: Using conserved 3D folds to study the evolution of rapidly evolving peptides

2016

Journal Article

Development of a μO-conotoxin analogue with improved lipid membrane interactions and potency for the analgesic target NaV1.8

Deuis, Jennifer R, Dekan, Zoltan, Inserra, Marco C., Lee, Tzong-Hsien, Aguilar, Marie-Isabel, Craik, David J., Lewis, Richard J., Alewood, Paul F., Mobli, Mehdi, Schroeder, Christina I., Henriques, Sónia Troeira and Vetter, Irina (2016). Development of a μO-conotoxin analogue with improved lipid membrane interactions and potency for the analgesic target NaV1.8. Journal of Biological Chemistry, 291 (22), 11829-11842. doi: 10.1074/jbc.M116.721662

Development of a μO-conotoxin analogue with improved lipid membrane interactions and potency for the analgesic target NaV1.8

Current funding

  • 2024 - 2025
    A national network for magnetic resonance spectroscopy
    ARC Linkage Infrastructure, Equipment and Facilities
    Open grant
  • 2024 - 2027
    Defining a new family of sodium channel accessory proteins
    ARC Discovery Projects
    Open grant

Past funding

  • 2023 - 2024
    High-Resolution Electron Paramagnetic Resonance Imaging and Spectroscopy
    ARC Linkage Infrastructure, Equipment and Facilities
    Open grant
  • 2022 - 2025
    Autocyclases: A new class of self-cyclising proteins
    ARC Discovery Projects
    Open grant
  • 2021 - 2023
    Bivalent analgesics: rational design of selective ion channel inhibitors with optimised mechanism of action
    NHMRC IDEAS Grants
    Open grant
  • 2019 - 2022
    A new source of bivalent molecules from nature
    ARC Discovery Projects
    Open grant
  • 2019 - 2022
    Accessing structurally elusive states of sodium channels as novel analgesic targets
    NHMRC Project Grant
    Open grant
  • 2019
    Chemical Purification Network
    UQ Major Equipment and Infrastructure
    Open grant
  • 2019
    Imaging Mass Spectrometry at Higher Mass Resolution
    UQ Research Facilities Infrastructure Grants
    Open grant
  • 2019 - 2021
    Molecular basis and inhibition of TIR-domain function in Toll-like receptor and neuronal cell-death pathways
    NHMRC Project Grant
    Open grant
  • 2018
    High-throughput ion channel pharmacology
    UQ Major Equipment and Infrastructure
    Open grant
  • 2018
    In vivo optical imaging into the next generation
    UQ Research Facilities Infrastructure Grants
    Open grant
  • 2018
    Multichannel peptide synthesiser to accelerate UQ's biodiscovery pipeline and peptide drug development programs
    UQ Major Equipment and Infrastructure
    Open grant
  • 2017 - 2019
    Targeting voltage sensing for drug development
    UQ Development Fellowships
    Open grant
  • 2016 - 2017
    A nuclear magnetic resonance facility for modern molecular analysis
    ARC Linkage Infrastructure, Equipment and Facilities
    Open grant
  • 2016 - 2018
    A pharmacological approach to define the contribution of Nav1.7 to pain pathways
    NHMRC Project Grant
    Open grant
  • 2016 - 2018
    Characterization and inhibition of higher-order assembly signalling in Toll-like receptor pathways
    NHMRC Project Grant
    Open grant
  • 2016
    Patch-clamp electrophysiology platform for drug and insecticide discovery
    UQ Major Equipment and Infrastructure
    Open grant
  • 2015
    Protein Analysis Facility
    UQ Major Equipment and Infrastructure
    Open grant
  • 2015 - 2018
    Understanding how toxins interact with lipid membranes and ion channels
    NHMRC Project Grant
    Open grant
  • 2014 - 2017
    Unravelling the structural complexity of ancient Australian arthropod venoms
    ARC Discovery Projects
    Open grant
  • 2012 - 2016
    ASAP-NMR: A leap forward in structural studies of proteins using NMR spectroscopy
    ARC Future Fellowships
    Open grant
  • 2012 - 2014
    Rational development of novel analgesics for the treatment of chronic pain
    NHMRC Project Grant
    Open grant
  • 2010
    High-throughput identification and structural characterization of selective Nav1.7 channel ligands; a prime target in the treatment of pain
    UQ Early Career Researcher
    Open grant

Availability

Professor Mehdi Mobli is:
Available for supervision

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Supervision history

Current supervision

  • Doctor Philosophy

    Studies of complex biomolecular systems using advanced biochemical and biophysical techniques

    Principal Advisor

    Other advisors: Associate Professor Jeffrey Harmer

  • Doctor Philosophy

    Structural and functional characterisation of an orphan family of opioid peptides

    Principal Advisor

    Other advisors: Associate Professor Jody Peters

  • Doctor Philosophy

    The ASIC thumb domain as a channel proxy for identification of drug leads for the treatment of ischemic conditions

    Principal Advisor

    Other advisors: Dr Lachlan Rash

  • Doctor Philosophy

    Fast Acquisition Methods in Multidimensional NMR

    Principal Advisor

  • Doctor Philosophy

    Characterisation of the lipid dependent gating of voltage gated ion channels

    Principal Advisor

  • Doctor Philosophy

    Accessing structurally elusive states of sodium channels as novel analgesic targets

    Principal Advisor

    Other advisors: Professor Irina Vetter, Dr Thomas Durek

  • Doctor Philosophy

    Fast Acquisition Methods in Multidimensional NMR

    Principal Advisor

  • Doctor Philosophy

    Modulation of opioid catabolism by endogenous neuropeptides

    Principal Advisor

  • Doctor Philosophy

    Analysis of Complex Metabolomic Data

    Associate Advisor

  • Doctor Philosophy

    Understanding the function of sodium channel accessory proteins to develop new treatments for chronic pain

    Associate Advisor

    Other advisors: Dr Jennifer Deuis, Professor Irina Vetter

  • Doctor Philosophy

    Complex Data Analysis Problems in NMR-based Metabolomics

    Associate Advisor

  • Doctor Philosophy

    Structural and biochemical characterization of dual enzymatic activity of TIR domains from plant innate immune receptors

    Associate Advisor

    Other advisors: Dr Natsumi Maruta, Professor Bostjan Kobe

  • Doctor Philosophy

    Characterization of bivalency in disulfide-rich peptides

    Associate Advisor

    Other advisors: Professor Irina Vetter

  • Doctor Philosophy

    Discovery and characterisation of multi-valent peptides

    Associate Advisor

    Other advisors: Professor Irina Vetter

Completed supervision

Enquiries

Contact Professor Mehdi Mobli directly for media enquiries about:

  • Mechanism of voltage gating by voltage-gated ion channels
  • Structure guided drug design
  • Structure guided evolution of venom peptides

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