Fullerene inhibits beta-amyloid peptide aggregation.
We report that fullerene inhibits strongly the amyloid peptide aggregation at the early stage. It specifically binds to the central hydrophobic motif, KLVFF, of A beta peptides. The IC(50) value has been measured as 9 microM for both A beta(11-25) and A beta(1-40). On the other hand, a control experiment shows melatonin rather specifically binds to the C-terminus region. The IC(50) value of fullerene appears to be at least four times larger for A beta(1-40), compared with melatonin, and 15 times larger for A beta(11-25). This work shows that fullerene can be a promising candidate in search of AD therapeutics because it has the very high IC(50) value for A beta aggregation.
Kim
Jeong Eun
JE
Fluorescence Nanoscopy Laboratory, Department of Chemistry, Division of Molecular Life Sciences, Ewha Womans University, Seoul 120-750, South Korea.
Lee
Minyung
M
D000595:Amino Acid Sequence; D016229:Amyloid beta-Peptides / Q000037:antagonists & inhibitors* / Q000737:chemistry*; D000970:Antineoplastic Agents / Q000494:pharmacology; D001665:Binding Sites; D037741:Fullerenes / Q000737:chemistry* / Q000494:pharmacology*; D007700:Kinetics; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry*; D012680:Sensitivity and Specificity
D016229:Amyloid beta-Peptides; D000970:Antineoplastic Agents; D037741:Fullerenes; D010446:Peptide Fragments