Dr Blagojce Jovcevski

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 an Associate Investigator 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 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.