Axel Abelein

Axel Abelein

Assistant Professor | Docent
Visiting address: Blickagången 16, Neo, Flemingsberg, 14152 Hudding
Postal address: H7 Medicin, Huddinge, H7 CeRM Abelein, 171 77 Stockholm

Research

  • My research concerns protein self-assembly related to neurodegenerative
    diseases with the focus on characterization of protein structure and
    molecular mechanisms of self-assembly. The studies in our lab include a
    broad range of different techniques within biophysics, protein
    biochemistry and biomedicine. My current research focuses on the
    aggregation mechanisms of amyloid-β peptide (Aβ) fibril formation,
    associated to Alzheimer’s disease and inhibition mechanisms by the
    BRICHOS domain, a chaperone-like protein that is potential candidate to be
    implemented in Alzheimer’s disease treatment. Furthermore, another research
    line is the development of new expression and purification protocols for
    aggregation-prone proteins using a spider silk-derived solubility tag, where
    one possible application is the generation of new biomaterials.
    Please visit our group homepage for more information:
    https://ki.se/en/bionut/laboratory-for-protein-misfolding-and-assembly

Selected publications

Articles

All other publications

Grants

  • Swedish Research Council
    1 January 2024 - 31 December 2027
    Protein misfolding has been identified as the underlying molecular process found in several devastating neurodegenerative diseases, such as Alzheimer’s and Parkinson’s disease (AD/PD). Based on the aggregation behavior, the surface of AD and PD-associated amyloid fibrils has been suggested to act as a catalyzer for self-replication and generation of toxic oligomers. Specifically tailored molecular chaperones, such as the BRICHOS protein domain, were shown to bind to the amyloid fibrils and break this autocatalytic cycle, possibly by blocking specific aggregation hotspots on the fibrils surface.Here, we aim to elucidate structural features of these catalytic sites from diverse in vitro and in vivo-derived amyloid fibrils using an integrated approach of high-resolution techniques. This information will provide a detailed understanding of the generic molecular mechanisms of chaperone-amyloid interactions, which will open the possibility to specifically target aggregation hotspots by designer chaperones or other drugs. Other goals are to explore the potential of BRICHOS to transport biologic drugs over the blood-brain barrier (BBB), and to determine the seeding activity of samples from patients suffering from different neurodegenerative disorders, which could establish new diagnostic tools.
  • Swedish Research Council for Environment Agricultural Sciences and Spatial Planning
    1 January 2021 - 31 December 2024

Employments

  • Assistant Professor, Department of Medicine, Huddinge, Karolinska Institutet, 2024-2026

Degrees and Education

  • Docent, Karolinska Institutet, 2024

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