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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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Amyloid Fibrils03:03

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Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
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Transient small molecule interactions kinetically modulate amyloid β peptide self-assembly.

Axel Abelein1, Lisa Lang, Christofer Lendel

  • 1Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.

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Small organic molecules like Congo red and lacmoid form non-toxic co-aggregates with amyloid beta (Aβ). These weak, transient interactions prevent Aβ self-assembly into fibrils, suggesting therapeutic potential for protein aggregation diseases.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Neuroscience

Background:

  • Amyloid beta (Aβ) peptide aggregation is central to Alzheimer's disease pathogenesis.
  • Small organic molecules, including Congo red and lacmoid, can influence Aβ self-assembly.
  • Understanding these interactions is crucial for developing therapeutic strategies.

Purpose of the Study:

  • To investigate the co-assembly of amyloid beta (Aβ) with lacmoid and Congo red.
  • To characterize the nature and kinetics of these Aβ-dye interactions.
  • To explore the therapeutic implications of these weak binding interactions.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy to detect Aβ in co-aggregates.
  • Kinetic analysis to study the interaction dynamics.
  • Monitoring of amyloid fibril formation.

Main Results:

  • Aβ forms NMR-invisible, non-toxic co-aggregates with lacmoid and Congo red.
  • The co-aggregation process involves two distinct kinetic phases.
  • Only a small fraction of Aβ participates in co-aggregation at any given time.
  • These weak, transient interactions kinetically inhibit Aβ self-assembly into amyloid fibrils.

Conclusions:

  • Weak binding interactions with small molecules can effectively redirect Aβ aggregation.
  • Lacmoid and Congo red act as kinetic inhibitors of amyloid fibril formation.
  • These findings highlight the potential of weak binders as a therapeutic approach for protein aggregation disorders.