Blagojce Jovcevski

Dr Blagojce Jovcevski

Postdoctoral Fellow

School of Agriculture, Food and Wine

Faculty of Sciences

Eligible to supervise Masters and PhD - 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.

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  • Journals

    Year Citation
    2021 Nguyen, S., Jovcevski, B., Pukala, T. L., & Bruning, J. B. (2021). Nucleoside selectivity of Aspergillus fumigatus nucleoside-diphosphate kinase.. The FEBS journal, 288(7), 2398-2417.
    DOI Scopus1 WoS1 Europe PMC1
    2021 Sanders, H. M., Jovcevski, B., Marty, M. T., & Pukala, T. L. (2021). Structural and mechanistic insights into amyloid-β and α-synuclein fibril formation and polyphenol inhibitor efficacy in phospholipid bilayers. The FEBS Journal, [1]-[16].
    DOI
    2020 Jovcevski, B., Das, S., Smid, S., & Pukala, T. L. (2020). Polyphenol honokiol and flavone 2′,3′,4′-trihydroxyflavone differentially interact with α-synuclein at distinct phases of aggregation. ACS Chemical Neuroscience, 11(24), 4469-4477.
    DOI Scopus1
    2020 Sajid, M. S., Jovcevski, B., Pukala, T. L., Jabeen, F., & Najam-Ul-Haq, M. (2020). Fabrication of Piperazine Functionalized Polymeric Monolithic Tip for Rapid Enrichment of Glycopeptides/Glycans.. Anal Chem, 92(1), 683-689.
    DOI Scopus5 WoS6
    2020 Sanders, H. M., Jovcevski, B., Carver, J., & Pukala, T. L. (2020). The molecular chaperone β-casein prevents amorphous and fibrillar aggregation of α-lactalbumin by stabilisation of dynamic disorder. Biochemical Journal, 477(3), 629-643.
    DOI Scopus7 WoS6 Europe PMC3
    2020 Wang, C. R., Bubner, E. R., Jovcevski, B., Mittal, P., & Pukala, T. L. (2020). Interrogating the higher order structures of snake venom proteins using an integrated mass spectrometric approach.. J Proteomics, 216, 103680.
    DOI Scopus1 WoS2 Europe PMC2
    2020 Horsley, J. R., Jovcevski, B., Wegener, K. L., Yu, J., Pukala, T. L., & Abell, A. (2020). Rationally Designed Peptide-Based Inhibitor of Aβ42 Fibril Formation and Toxicity: A Potential Therapeutic Strategy for Alzheimer's Disease.. Biochem J, 477(11), 2039-2054.
    DOI Scopus5 WoS5 Europe PMC3
    2020 Yeoh, Y. Q., Horsley, J., Yu, J., Polyak, S. W., Jovcevski, B., & Abell, A. D. (2020). Short photoswitchable antibacterial peptides. ChemMedChem, 15(16), 1505-1508.
    DOI Scopus5 WoS5
    2020 Salman Sajid, M., Jovcevski, B., Mittal, P., Fatima, B., Hussain, D., Jabeen, F., . . . Najam-ul-Haq, M. (2020). Glycosylation heterogeneity and low abundant serum glycoproteins MS analysis by boronic acid immobilized Fe<inf>3</inf>O<inf>4</inf>@1,2-Epoxy-5-Hexene/DVB magnetic core shell nanoparticles. Microchemical Journal, 159, 8 pages.
    DOI Scopus2
    2019 Liu, Y., Jovcevski, B., & Pukala, T. L. (2019). C-Phycocyanin from Spirulina Inhibits α-synuclein and amyloid-β fibril formation but not amorphous aggregation. Journal of Natural Products, 82(1), 66-73.
    DOI Scopus8 WoS8 Europe PMC4
    2018 Jovcevski, B., Andrew Aquilina, J., Benesch, J., & Ecroyd, H. (2018). The influence of the N-terminal region proximal to the core domain on the assembly and chaperone activity of αB-crystallin. Cell Stress and Chaperones, 23(5), 827-836.
    DOI Scopus6 WoS6 Europe PMC4
    2017 Jovcevski, B., Kelly, M., Aquilina, J., Benesch, J., & Ecroyd, H. (2017). Evaluating the effect of phosphorylation on the structure and dynamics of Hsp27 dimers by means of ion mobility mass spectrometry. Analytical Chemistry, 89(24), 13275-13282.
    DOI Scopus6 WoS8 Europe PMC3
    2015 Jovcevski, B., Kelly, M., Rote, A., Berg, T., Gastall, H., Benesch, J., . . . Ecroyd, H. (2015). Phosphomimics destabilize Hsp27 oligomeric assemblies and enhance chaperone activity. Chemistry and Biology, 22(2), 186-195.
    DOI Scopus69 WoS69 Europe PMC53
    2015 Cork, A., Ericsson, D., Law, R., Casey, L., Valkov, E., Bertozzi, C., . . . Kobe, B. (2015). Stability of the octameric structure affects plasminogen-binding capacity of streptococcal enolase. PLoS ONE, 10(3), e0121764-1-e0121764-18.
    DOI Scopus6 WoS7 Europe PMC4
    2013 Henningham, A., Ericsson, D., Langer, K., Casey, L., Jovcevski, B., Singh Chhatwal, G., . . . Walker, M. (2013). Structure-informed design of an enzymatically inactive vaccine component for group A Streptococcus. mBio, 4(4), e00509-13-1-e00509-13-9.
    DOI Scopus18 WoS15 Europe PMC8
  • Book Chapters

    Year Citation
    2019 Jovcevski, B., & Pukala, T. (2019). Mass Spectrometry and Its Applications. In V. Ramesh (Ed.), Biomolecular and Bioanalytical Techniques Theory, Methodology and Applications (pp. 219-253). USA: Wiley.
  • 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)
  • Position: Postdoctoral Fellow
  • Phone: 83134903
  • Email: blagojce.jovcevski@adelaide.edu.au
  • Fax: 8313 4380
  • Campus: North Terrace
  • Building: Molecular Life Sciences, floor 1
  • Room: 1.49
  • Org Unit: Chemistry

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