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.