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

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 structu...

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Bibliographic Details
Published in:Chemical communications (Cambridge, England) England), 2018, Vol.54 (56), p.7762-7765
Main Authors: Malishev, Ravit, Arad, Elad, Bhunia, Susanta Kumar, Shaham-Niv, Shira, Kolusheva, Sofiya, Gazit, Ehud, Jelinek, Raz
Format: Article
Language:English
Subjects:
Alzheimer's disease
Amyloid beta-Peptides - chemistry
Amyloid beta-Peptides - toxicity
Carbon - chemistry
Carbon dots
Cell Line, Tumor
Cytotoxicity
Fibrillation
Humans
Lipid Bilayers - chemistry
Lysine
Lysine - chemistry
Morphology
Particle Size
Peptide Fragments - chemistry
Peptide Fragments - toxicity
Protein Aggregates
Protein Conformation, beta-Strand
Protein Multimerization
Quantum Dots - chemistry
Stereoisomerism
Toxicity
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Summary: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.
ISSN:1359-7345
1364-548X
DOI:10.1039/c8cc03235a