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All-D-peptide D3 binds to amyloid-beta (Aβ) monomers, slowing Alzheimer's-associated Aβ42 fibrillation. This study reveals how D3 modulates Aβ nucleation, offering insights into intrinsically disordered protein interactions.

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D-enantiomeric peptideaggregationamyloid-β peptidescomplex formationintrinsically disordered protein

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Area of Science:

  • Biochemistry
  • Neuroscience
  • Drug Discovery

Background:

  • Alzheimer's disease is linked to amyloid-beta (Aβ) peptide aggregation.
  • Intrinsically disordered proteins like Aβ present challenges for studying ligand interactions.
  • All-D-peptides offer high specificity and metabolic stability for drug development.

Purpose of the Study:

  • To characterize the interaction between the all-D-peptide D3 and Aβ42 monomers.
  • To investigate how D3 binding affects Aβ42 aggregation and fibrillation.
  • To elucidate the molecular mechanism of D3's influence on Aβ assemblies.

Main Methods:

  • Characterization of D3-Aβ42 monomer interactions.
  • Stoichiometry analysis of D3-Aβ42 complexes.
  • Assessment of D3's effect on Aβ42 β-sheet formation and fibrillation kinetics.

Main Results:

  • D3 binds Aβ42 monomers with submicromolar affinity.
  • D3 and Aβ42 form complexes with varying stoichiometries (e.g., 1:1).
  • Substoichiometric D3 concentrations significantly inhibit Aβ42 fibrillation by modulating nucleation.

Conclusions:

  • D3 is a potent inhibitor of Aβ42 aggregation.
  • D3's mechanism involves interference with the Aβ42 nucleation phase.
  • This work advances understanding of intrinsically disordered protein interactions and potential therapeutic strategies for Alzheimer's disease.