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
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Amyloid beta-Peptides / chemistry*
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Amyloid beta-Peptides / toxicity
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Carbon / chemistry*
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Cell Line, Tumor
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Humans
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Lipid Bilayers / chemistry
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Lysine / chemistry
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Particle Size
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Peptide Fragments / chemistry*
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Peptide Fragments / toxicity
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Protein Aggregates
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Protein Conformation, beta-Strand
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Protein Multimerization
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Quantum Dots / chemistry*
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Stereoisomerism
Substances
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Amyloid beta-Peptides
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Lipid Bilayers
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Peptide Fragments
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Protein Aggregates
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amyloid beta-protein (1-42)
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Carbon
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Lysine