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A/Prof. Mark Hackett

Associate Professor
School of Molecular and Life Sciences

Neuro-metallomics research group

I have always been driven by curiosity and a passion for understanding the world at a molecular level. My strong analytical mindset and fascination with instrumentation led me to study analytical chemistry at university. Over time, my deep interest in biology, particularly the mysteries of life, inspired me to apply these skills to explore complex biological systems. Combining analytical chemistry and advanced microscopy techniques to study biological processes has been both intellectually stimulating and personally rewarding.  

About

A/Prof. Mark Hackett is motivated by the growing need to maintain quality of life as medical advances continue to extend human lifespan. His research focuses on understanding the molecular processes that occur in the ageing brain, with the aim of preserving cognitive function and reducing the impact of neurodegenerative diseases that can threaten an individual’s sense of self.


A/Prof. Mark Hackett is an analytical and bioinorganic chemist whose work examines the role of metal ions in health and disease. His research team develops advanced X ray imaging tools to visualise metal homeostasis in the brain, with a particular focus on iron, copper and zinc. Through this work, the team seeks to uncover the pathways through which metal ions contribute to neurological and neurodegenerative disorders. Synchrotron facilities, including the Australian Synchrotron at ANSTO, play a central role in supporting this research program.


A/Prof. Mark Hackett completed his PhD at the University of Sydney in 2011. He then undertook postdoctoral research at the University of Saskatchewan in Canada, supported by fellowships from the Saskatchewan Health Research Foundation and the Canadian Institutes of Health Research. In 2016, he returned to Australia to establish his independent research group at Curtin University. Since then, his work has been supported by an ARC Future Fellowship, an ARC Discovery Project, and research grants from the Dementia Australia Research Foundation and Multiple Sclerosis Australia.


Specialty areas:

 
  • American Chemical Society
  • Royal Australian Chemical Institute
  • Australasian Neuroscience Society

Email: Mark.J.Hackett@curtin.edu.au
Tel: +61 (08) 9266 3102
ORCID
Google Scholar
Curtin Staff Profile

 

Research Focus

A/Prof. Mark Hackett’s research focuses on developing and refining advanced elemental and biomolecular imaging techniques to better understand brain function and disease. His work utilises a range of spectroscopic approaches, including Fourier Transform Infrared (FTIR) spectroscopy, Raman spectroscopy, X ray fluorescence microscopy (XFM), and X ray absorption spectroscopy (XAS). Working closely with neuroscientists, A/Prof. Hackett and his team apply these techniques to investigate the molecular and elemental mechanisms that underpin both healthy and diseased brain states.


Beyond neuroscience, A/Prof. Mark Hackett’s analytical expertise extends across several disciplines, including forensic science, plant science, and microbiology, where similar imaging and spectroscopic approaches are applied to address complex biological questions.


A significant component of A/Prof. Mark Hackett’s research involves the use of synchrotron light sources, particularly the Australian Synchrotron. He is a frequent user of this facility and currently serves as Chair of the X ray Fluorescence Microscopy Program Committee. He also contributes to the broader synchrotron community through his roles on two beamline advisory panels and the User Advisory Committee.


Within his research group, A/Prof. Hackett leads efforts to develop new analytical and imaging protocols to investigate the role of metal ions in brain health and disease. In particular, the team focuses on understanding how iron, copper, and zinc contribute to maintaining normal brain function and how disruptions in their regulation may contribute to neurological disorders.

Research Team

Dr Gaewyn Ellison

Research Fellow

Dr Elena Dallerba

University Associate

Meg Williams

PhD Student

David Hartnell

PhD Student

Publications

ABSTRACT

This study demonstrates the thermal, structural, and rheological properties of flours and protein isolates of five Lupinus angustifolius L. varieties using soy flour and protein isolate as references. Fourier transform infrared (FTIR) analysis of lupin protein isolates in the amide I region revealed significantly higher β-sheet content than α-helices, together comprising ∼50% of the secondary protein structures. In differential scanning calorimetry (DSC), lupin flour exhibited two distinct peak denaturation temperatures (Td), first between 90 and 91°C, second between 103 and 105°C. Similarly, for lupin protein isolates, the two Tds were at 84–86°C and 96–98°C, which represent β-conglutin and α-conglutin, respectively. The microstructure of lupin proteins was less interconnected than soy, which had a more compact and continuous protein network. Lupin protein isolates form a weaker and easily deformed gel network compared to soy protein isolates due to their lower complex viscosity (ŋ∗), storage (G′) and loss (G") moduli, and higher loss factor (tan δ) compared to soy protein isolates. Flours were characterised as more frequency-dependent than protein isolates, indicating weaker gel networks. Rapid viscosity analyser (RVA) profiles revealed that lupin flours exhibited higher peak (237.00–265.00 cP) and final viscosities (3.38–4.89 cP) than soy flour (166.33 cP and 1.11 cP, respectively), indicating the influence of non-starch components on enhanced pasting properties in lupin flours. Since lupin proteins form weaker gels than soy, process modulations are essential to improve their functionality in food products. Moreover, higher Td associated with lupin flour over soy flour demonstrate greater thermal stability, which is potentially beneficial in heat-processed, high-protein products.

Wanniarachchi, P. C., M. Mocerino, M. J. Hackett, M. Nesbit, G. Shea, and R. Coorey. 2026.Comparative analysis of thermal, structural and rheological properties of protein isolates and kernel flour from Australian sweet lupin varieties using soy as a reference.Food Hydrocolloids 172 (2)
ABSTRACT

Coordination of N1 and N2-methylated regioisomers of 2-(1H-tetrazol-5-yl)pyridine and 2-(1H-tetrazol-5-yl)quinoline to ReBr(CO)3 and Ir(ppy)2+ (ppy = cyclometalated 2-phenylpyridine) fragments resulted in the isolation of a small family of Re(I) and Ir(III) luminescent complexes. The complexes display phosphorescent emission from their triplet ligand-to-metal charge transfer excited states in degassed solution at room temperature. Notably, the position of the methyl substituent has a profound effect on the photophysical properties. The N1-methylated complexes in all cases display a significant redshift in the emission band. The shift is ascribed to a stabilisation of the π* orbitals of the tetrazole ligands, which is also supported by cyclic voltammetry and time-dependent density functional theory (TD-DFT) calculations. The complexes were used as luminescent labels for the staining of mouse brain tissue. The Re(I) complexes did not show any evident staining. On the other hand, the Ir(III) complexes – particularly those bound to the ligand containing the quinoline substituent – demonstrated affinity for lipid-rich myelinated regions in brain tissues and white matter in cerebellum tissues. The specificity of the Ir(III) complexes was further demonstrated by means of correlative optical microscopy and Fourier transform infrared (FTIR) microscopy.

Dallerba, E., L. J. Cameron, B. I. Armstrong, G. Ellison, E. Turner, E. S. Innes, G. L. Strickling, J. Pangiarella, P. Conghaile, M. Nesbit, and 6 more contributors. 2026. Methylated regioisomers of Re(i) and Ir(iii) tetrazole complexes: photophysical properties and optical imaging of brain tissue.Dalton Transactions 55 (1): 183-195.

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