Chiral modulation of amyloid beta fibrillation and cytotoxicity by enantiomeric carbon dots

Chem Commun (Camb). 2018 Jul 10;54(56):7762-7765. doi: 10.1039/c8cc03235a.

Abstract

Enantiomeric carbon dots (C-dots) synthesized from l-lysine or d-lysine, modulate aggregation and cytotoxicity of amyloid beta-42 (Aβ42), the primary constituent of the amyloid plaques associated with Alzheimer's disease. In particular, l-Lys-C-dots dramatically remodeled Aβ42 secondary structure and fibril morphologies, as well as inhibited Aβ42 cytotoxicity and membrane interactions.

MeSH terms

  • Amyloid beta-Peptides / chemistry*
  • Amyloid beta-Peptides / toxicity
  • Carbon / chemistry*
  • Cell Line, Tumor
  • Humans
  • Lipid Bilayers / chemistry
  • Lysine / chemistry
  • Particle Size
  • Peptide Fragments / chemistry*
  • Peptide Fragments / toxicity
  • Protein Aggregates
  • Protein Conformation, beta-Strand
  • Protein Multimerization
  • Quantum Dots / chemistry*
  • Stereoisomerism

Substances

  • Amyloid beta-Peptides
  • Lipid Bilayers
  • Peptide Fragments
  • Protein Aggregates
  • amyloid beta-protein (1-42)
  • Carbon
  • Lysine