Blagojce Jovcevski

Dr Blagojce Jovcevski

Postdoctoral Fellow

School of Agriculture, Food and Wine

Faculty of Sciences

Eligible to supervise Masters and PhD (as Co-Supervisor) - email supervisor to discuss availability.

Blagojce completed his PhD at the University of Wollongong in 2017, under the supervision of Prof. Heath Ecroyd focusing on understanding the structure-function relationship of small heat-shock proteins, which are associated with numerous neurodegenerative diseases including Alzheimer's disease, Parkinson's disease and amyotrophic lateral sclerosis, using native mass spectrometry and biophysical approaches.

Blagojce joined the University of Adelaide in late 2017 in the Department of Chemistry (School of Physical Sciences) and also joined the Department of Agricultural Science (School of Agriculture, Food and Wine) in 2020.

Blagojce is a Postdoctoral Research Fellow working with Assoc. Prof. Tara Pukala (School of Physical Sciences, Adelaide Proteomics Centre) to utilise mass spectrometry-based techniques to understand the aggregation dynamics of α-synuclein in various lipid environments. In addition, Blagojce is also working on characterising the structure and dynamics of transmembrane chitin synthases using native ion mobility - mass spectrometry with Prof. Vincent Bulone (School of Agriculture, Food and Wine, Adelaide Glycomics). Blagojce is also apart of the research team for the Research Consortium Program for Agriculture Product Development which is supported by the South Australia Department for Industry and Skills. 

Investigating the structural dynamics of amyloidogenic proteins using mass spectrometry-based approaches

The pathogenesis of neurodegenerative diseases, such as Alzheimer’s disease, Parkinson's disease and amyotrophic lateral sclerosis, is believed to be caused by the aggregation of non-native proteins. One such protein that forms fibril (amyloid) aggregates is alpha-synuclein, which is heavily associated with Parkinson's disease. My current focus is on understanding the role lipids play in the aggregation dynamics of alpha-synuclein using a range of mass spectrometry-based approaches. Native MS is a high-resolution tool utilised in structural biology which can define a range of structural features within proteins, such as oligomeric distribution and polydispersity, unfolded/unstructured states, assembly stability and quaternary conformation of proteins. Using these techniques, in conjunction with other biophysical tools, can provide a structural rationale for protein function/dysfunction. 

Development of novel peptide-based protein aggregation inhibitors and enzymatic-targetting antimicrobials

My work has also facilitated structure-informed design of peptide-based inhibitors of amyloid fibril formation as potential therapeutics of diseases where protein misfolding and aggregation are central, as well as enzymatic inhibitor screening of novel antimicrobial drugs targeting bacterial and fungal pathogens in collaboration with Prof. Andrew Abell, Dr. John Bruning and The Institute for Photonics and Advanced Sensing (IPAS)

Utilising MS approaches as a complementary tool in structural biology and structure-activity relationships

We continuely utilise MS-based approaches to complement traditional structural biology approaches (e.g. X-ray crystallography, cryo-EM, NMR) to structurally rationalise biomolecular function/activity to guide antifungal drug design and vaccine design against infectious disease. In addition, these approaches have been crucial in discovering venom proteomes and their role in envenomation and developing novel glycopeptide enrichment stratergies for disease diagnostics. 

Characterising transmembrane proteins using native ion-mobility MS

This project aims to understand the mechanisms and key enzymes that control cell wall stability and biosynthesis in the fish pathogen Saprolegnia parasitica. Using native ion-mobility MS allows these dynamic membrane proteins to be studied and aid in the development of novel strategies for disease control in aquaculture, as well as crop protection from related plant pathogens with Adelaide Proteomics Centre and Adelaide Glycomics.

  • 2019: Postdoctoral Travel Award, Lorne Conference on Protein Structure and Function (valued at $250)
  • 2018: Australian Bicentennial Fellowship Travel Award, Menzies Australian Institute (valued at $1,800)
  • 2015: American Society of Mass Spectrometry Asilomar Conference on Native Mass Spectrometry Travel Award, American Society of Mass Spectrometry (valued at $1,500)
  • 2013: Faculty of Science, Medicine and Health Travel Award (research visit to University of Oxford), University of Wollongong (valued at $3,000)
  • 2012-2016: Henning Family Foundation PhD Scholarship, Australian Rotary Health (3.5 years valued at $101,500)
  • Current Higher Degree by Research Supervision (University of Adelaide)

    Date Role Research Topic Program Degree Type Student Load Student Name
    2021 Co-Supervisor Investigating the formation, inhibition and detection of amyloid oligomers in the context of neurodegenerative disease Master of Philosophy Master Full Time Mr Shaun Thomas Ellis
    2020 Co-Supervisor Mass Spectrometric Characterisation of Protein Assemblies from Snake Venom Master of Philosophy Master Full Time Miss Emily Rose Bubner
    2020 Co-Supervisor Biochemistry Doctor of Philosophy Doctorate Full Time Ms Stephanie Nguyen
  • Position: Postdoctoral Fellow
  • Phone: 83134903
  • Email:
  • Fax: 8313 4380
  • Campus: North Terrace
  • Building: Molecular Life Sciences Building, floor 1
  • Room: 1.49
  • Org Unit: Chemistry

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