Victor Streltsov has received Master’s Degree in Physical Chemistry and Physics at Mendeleev University of Chemical Technology of Russia (MUCTR, Moscow) and Moscow State University (1982), and PhD in Physics and Mathematics with specialisation in Crystallography and Crystal Physics at MUCTR (1986). His has been further trained in the Biomolecular Structures Laboratory (Acad BK Vainstein) of the Institute of Crystallography of Russian Academy of Science and the University of Western Australia (UWA Postdoctoral award, Crystallography Centre, Dr EN Maslen). In 2002 he joined CSIRO and was a stream (group) leader in the Neurodegenerative disease theme of the CSIRO Preventative Flagship running projects in diagnostic, imaging and neuroprotective agents, using structure-based design methods closely collaborating with the Florey Institute of Neuroscience and Mental Health (Prof CL Masters), The University of Melbourne. He was a Visiting Researcher/Professor at Chalmers University of Technology (Sweden) and JSPS fellow at Tokyo Institute of Technology (Japan). He was an Honorary Professorial Fellow at Florey Institute and Physics Department of the University of Melbourne. He is currently conducting structural studies of proteins involved in neurodegenerative diseases at Florey Institute and a specially appointed Professor at the Tokyo Institute of Technology (Tokyo, Japan) with Prof H. Kawaji’s group. Prof Streltsov has а broad expertise in synchrotron structural studies of various types of materials from minerals, small and macro-molecules to cells, tissues and animal brains in the fields of charge density, protein crystallography, x-ray spectroscopy, small/wide angle x-ray scattering, x-ray imaging and cryo-EM.

It will extend my collaboration with Tokyo Tech initiated many years ago. It will also help to establish contacts with other researchers and major research centers in Japan. My current structure-based research in neurodegeneration will benefit from interdisciplinary research conducted at WHRI with investigators from different areas of specialized knowledge and skill.

• Normal and abnormal pathways in Amyloid-beta and Tau-protein.

  Collaborative research plan involves synchrotron x-ray studies (crystallography, spectroscopy) and electron microscopy (cryo-EM) of amyloid-β (Aβ) peptide and Tau-protein oligomers to better understand the process of filament formation and fibril elongation (nanostructures), with focus on effects of metals (Fe, Cu, Zn) on amyloid aggregation. Aggregation leads to an increase in thermal stability linked to the typical conformation transition to a β-hairpin and a cross-β structure. Amyloid proteins by nature are display a high level of thermal stability, due to the thermo-dynamically favourable state of the aggregated form.
  Within this context we propose to investigate thermodynamic properties of fibril and filament materials in collaboration with the Materials and Structures Laboratory (MSL) at the Tokyo Tech WHRI. MSL aims to create innovative materials with outstanding properties and functions through interdisciplinary research efforts merging the fields of inorganic materials, metals and (bio)organic materials.
  Proposed studies of Aβ and Tau proteins are significant and important, since these proteins play a major role in developing Alzheimer’s disease (AD). AD is a progressive neurodegenerative disorder that is characterized by the presence of Aβ fibrils and tau filaments in the brain. AD is the most common cause of dementia (up to 80%) and its prevalence is increasing in Japan and around the world and there are currently no disease modifying drugs for its treatment.
  
  - Periods: 2019-2022
  
  - Members: Florey Institute of Neuroscience and Mental Health and School of Physics of the University of Melbourne (Australia), Materials and Structures laboratory of Tokyo Tech and WHRI.
  

  Amyloid-beta Tau-protein Amyloid-beta structure Tau-filament formation