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Multiple assembly pathways underlie amyloid-beta fibril polymorphisms.

Claire Goldsbury1, Peter Frey, Vesna Olivieri

  • 1M.E. Müller-Institute for Structural Biology, Biozentrum, University of Basel, CH-4056 Basel, Switzerland.

Journal of Molecular Biology
|August 13, 2005
PubMed
Summary
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Amyloid beta-protein forms various fibril types through multiple assembly pathways. Researchers identified distinct protofibril and mature fibril structures and their growth rates, suggesting complex formation mechanisms.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Neuroscience

Background:

  • Amyloid beta-protein (Aβ) aggregation is central to Alzheimer's disease pathogenesis.
  • Aβ forms diverse structures, including oligomers, protofibrils, and mature fibrils, but their relationships are unclear.
  • Understanding these species is crucial for developing therapeutic strategies.

Purpose of the Study:

  • To elucidate the precursor-to-product relationships among different amyloid beta-protein species.
  • To characterize the structural and dynamic properties of protofibrils and mature fibrils.
  • To investigate the assembly pathways leading to polymorphic fibril formation.

Main Methods:

  • Scanning transmission electron microscopy (STEM) to measure mass-per-length (MPL) of fibrils.

Related Experiment Videos

  • Time-lapse atomic force microscopy (AFM) to determine fibril elongation rates.
  • In vitro incubation of amyloid beta-protein to generate various aggregated species.

    • Main Results:

    • Protofibrils (19 kDa/nm) and two mature fibril types (18 kDa/nm and 27 kDa/nm) were identified.
    • The 18 kDa/nm fibrils, morphologically distinct, share MPL with protofibrils, suggesting conformational changes.
    • The 27 kDa/nm fibrils have a significantly higher MPL, indicating different assembly pathways or subunits.
    • Fibril elongation rates varied, with mature fibrils growing much faster than protofibrils.

    Conclusions:

    • Multiple, concurrent assembly pathways likely contribute to the polymorphism of amyloid beta-protein fibrils.
    • Protofibrils may transform into certain mature fibril types, while others arise independently.
    • The distinct structural and kinetic properties of these species offer insights into aggregation mechanisms.