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) 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). 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. 

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.

Development of novel peptide-based protein aggregation inhibitors

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 (in collaboration with Prof. Andrew Abell research group). 

  • 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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