Dr Blagojce Jovcevski

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).