Mekanismer för proteinaggregering och -inhibering – Axel Abeleins grupp

Felveckning av proteiner och bildning av kors-β-strukturerade amyloidfibriller är kopplade till många neurodegenerativa störningar men är också byggstenarna i nya biomaterial. Vår forskning syftar till att förstå de underliggande mekanismerna för amyloidbildning för att både hitta behandlingsstrategier mot demenssjukdomar, särskilt Alzheimers sjukdom, och för att utveckla nya proteinbaserade material.

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För detaljerad information om vår forskning, se vår engelska sida.

Publikationer

Utvalda publikationer

Finansiering

Forskningsbidrag

  • 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

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