Blagojce Jovcevski

Dr Blagojce Jovcevski

Externally-Funded Research Fellow (B)

School of Biological Sciences

Faculty of Sciences, Engineering and Technology

Eligible to supervise Masters and PhD - email supervisor to discuss availability.


Blagojce completed his PhD at the University of Wollongong in 2017 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 (ALS, motor neuron disease), using native mass spectrometry and biophysical approaches.

Blagojce joined the University of Adelaide in late 2017 as a Postdoctoral Research Associate working with Prof. Tara Pukala (Discipline of Chemistry, School of Physics, Chemistry and Earth Sciences) to utilise mass spectrometry-based techniques to understand the aggregation dynamics of amyloid-fibril forming proteins and their effects on proteostasis. In addition, 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 (2020-2023).

In 2023, Blagojce joined the Discipline of Molecular & Biomedical Science (School of Biological Sciences) and established the Proteostasis and Disease Research Group - a multidisciplinary team focusing on the mechanisms and molecular networks regulating protein homeostasis (proteostasis) in several cell types (gut and the brain) and their contribution to neurodegenerative diseases including Parkinson’s disease and ALS, through funding from The Hospital Research Foundation.

Research Overview

Understanding proteostasis mechanisms in the gut-brain axis in Parkinson's disease and motor neuron disease

The pathogenesis of neurodegenerative diseases, such as Parkinson's disease and amyotrophic lateral sclerosis, is believed to be caused by the aggregation of non-native proteins. Protein aggregation is due to the failure of protien homeostasis (proteostasis) mechanisms to maintain protein foldedness and effectively clear protein aggregates. My group focuses on understanding the molecular mechanisms that maintain proteostasis in the gut-brain axis and how issues in this network fail to prevent protein aggregation in the gut, leading to proteinopathies namely Parkinson's disease and Amyotrophic Lateral Sclerosis (ALS). 

Bioactive profiling of high-value commerical and biomedical products from problematic waste biomass

Food waste in Australia is an ever-present economical and environmental issue, costing the Australian economy $37 billion annually with 7.6 million tonnes of food wasted per year and contributing up to 3% to Australia's greenhouse-gas emmisions. Transforming these waste streams to new viable products is therefore vital. I have been utilising analytical chemistry approaches to identify the composition of bioactives in these waste streams and profiling their bioactivities (neuroprotective, antimicrobial, antiviral) to guide the production of commercial and biomedical products through the Research Consortium Program for Agriculture Product Development.

Investigating the structural dynamics of amyloidogenic proteins using mass spectrometry-based approaches

My 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. 

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 native MS tools 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 understand molecular chaperone function in proteostasis and guide antifungal and vaccine design against infectious disease.

 

Prospective Projects (Honours/Masters/PhD)

Project 1

Title: Developing gut-brain axis cell models mimicking synucleinopathies

Description: Synucleinopathies such as Parkinson’s disease (PD) and dementia with Lewy bodies arise from the formation of intracellular toxic protein aggregates. Formation of α-synuclein aggregates in the gut are trafficked from gut epithelial cells to CNS neurons during disease. This project involves 1) establishing gut and neuronal cell models (as well as mixed cell models) of α-synuclein aggregation, 2) assess the global molecular changes during α-synuclein aggregation, and 3) high-throughput screening of potential drug leads and probing aggregate trafficking mechanisms across cell types.

Location(s): Molecular Life Sciences/Adelaide Microscopy, North Terrace Campus

Available for: Honours/PhD

 
Project 2

Title: Developing gut-brain axis cell models of amyotrophic lateral sclerosis

Description: Amyotrophic lateral sclerosis (ALS), also known as motor neuron disease (MND), also arises from the formation of toxic aggregates of proteins including SOD1 and TDP-43. This project involves 1) establishing gut and neuronal cell models (as well as mixed cell models) of SOD1 and TDP-43 aggregation, 2) assess the global molecular changes during the aggregation of proteins associated with ALS, and 3) high-throughput screening of potential drug leads and probing aggregate trafficking mechanisms across cell types.

Location(s): Molecular Life Sciences/Adelaide Microscopy, North Terrace Campus

Available for: Honours/PhD

 
Project 3

Title: Establishing the amyloid interactome (aggregome) in the gut-brain axis

Description: Identifying the molecular networks formed during protein aggregation is crucial for biomarker discovery and precision medicine approaches. This project involves 1) the mapping of aggregating protein interactions in gut and neuronal cell models (as well as mixed cell models) of α-synuclein, SOD1 and TDP-43 aggregation.

Location(s): Molecular Life Sciences, North Terrace Campus

Available for: Honours/Masters

 

 

Year Funding Source Amount (AUD)
2024

Biochemistry Research Foundation Trust Fund - EMCR Project Grant: Discovering drug leads in brewing waste to treat motor neuron disease

$35,000
2023-26

The Hospital Research Foundation Group - EMCR Research Fellowship (Sole CI): Developing gut-brain axis cell models to probe proteostasis deficits triggering neurodegeneration

$390,000
2019 Postdoctoral Travel Award - Lorne Conference on Protein Structure and Function (Sole CI) $250
2018 Australian Bicentennial Fellowship Travel Award - Menzies Australian Institute (Sole CI) $1,800
2015 American Society of Mass Spectrometry Asilomar Conference on Native Mass Spectrometry Travel Award -American Society of Mass Spectrometry (Sole CI) $1,500
2013-14 Faculty of Science, Medicine and Health Travel Award - University of Wollongong (Sole CI) $3,000
2012-16 Henning Family Foundation PhD Scholarship - Australian Rotary Health (Sole CI) $101,500
Lecturer: Biochemistry II - Molecular & Cellular Biology, Semester 1

Protein structure and function

Transport proteins and enzyme kinetics

Lecturer: Biochemistry III - Molecular & Structural Biology, Semester 1

Protein Lifecycle & Protein quality control

Membrane and protein trafficking

  • 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
  • Past Higher Degree by Research Supervision (University of Adelaide)

    Date Role Research Topic Program Degree Type Student Load Student Name
    2020 - 2021 Co-Supervisor Mass Spectrometric Characterisation of Protein Assemblies from Bitis arietans Snake Venom Master of Philosophy Master Full Time Miss Emily Rose Bubner
    2020 - 2021 Co-Supervisor Structural and Biochemical Insights into Antifungal Drug Targets from Aspergillus fumigatus Doctor of Philosophy Doctorate Full Time Ms Stephanie Nguyen
  • Mentoring

    Date Topic Location Name
    2022 - ongoing Diagnosis and therapeutics of intrinsically disordered protein misfolding disorders Doctor of Philosophy - University of Adelaide Mr Zohaib Raza
    2021 - ongoing Chemical and Functional Exploration of Agricultural Waste for Identification of High Value Bioactives Doctor of Philosophy - University of Adelaide Mr River Jack Pachulicz
    2020 - ongoing Structural characterisation of snake venom proteins by mass spectrometry Doctor of Philosophy - University of Adelaide Miss Chia-De Ruth Wang
    2020 - ongoing Biophysical characterisation of DNA triplexes for antigene technology Doctor of Philosophy - University of Adelaide Mr Jack Klose
    2020 - 2023 The Synthesis and Activity of New Antibiotics Doctor of Philosophy - University of Adelaide Dr Damian Stachura
    2019 - 2020 Functionalised polymers for glycopeptide enrichment Doctor of Philosophy - Bahauddin Zakariya University (Pakistan) Mr Muhammad Salman Sajid
    2017 - 2021 MASS SPECTROMETRY-BASED STRUCTURAL INSIGHTS INTO PROTEIN ASSEMBLIES Doctor of Philosophy - University of Adelaide Mr Henry Michael Sanders
  • Position: Externally-Funded Research Fellow (B)
  • Phone: 83134903
  • Email: blagojce.jovcevski@adelaide.edu.au
  • Fax: 83134380
  • Campus: North Terrace
  • Building: Molecular Life Sciences, floor 1
  • Org Unit: Molecular and Biomedical Science

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