Dr Blagojce Jovcevski
Blagojce Jovcevski completed his PhD at the Illawarra Health and Medical Research Institute and the University of Wollongong in 2017, under the supervision of Assoc. Prof. Heath Ecroyd and Dr. Andrew Aquilina. His PhD project focused on studying the structure-function relationship of small heat-shock proteins, which are associated with numerous degenerative diseases, using native mass spectrometry.
Recently, I have joined the Pukala research group to utilise similar techniques to understand the aggregation dynamics of aggregation-prone proteins that are associated with neurodegenerative diseases.
Investigating the structure 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.
|2017||Postdoctoral Fellow||University of Adelaide|
|2012 - 2017||University of Wollongong||Australia||PhD|
|2007 - 2011||University of Wollongong||Australia||Bachelor of Science (Honours) (Biological Sciences)|
|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.
|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. B. Beall (Ed.). PLoS ONE, 10, 3, e0121764-1-e0121764-18.
|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.
|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.