Fullerene inhibits β-amyloid peptide aggregation

Abstract

We report that fullerene inhibits strongly the amyloid peptide aggregation at the early stage. It specifically binds to the central hydrophobic motif, KLVFF, of Aβ peptides. The IC50 value has been measured as 9μM for both Aβ11-25 and Aβ1-40. On the other hand, a control experiment shows melatonin rather specifically binds to the C-terminus region. The IC50 value of fullerene appears to be at least four times larger for Aβ1-40, compared with melatonin, and 15 times larger for Aβ11-25. This work shows that fullerene can be a promising candidate in search of AD therapeutics because it has the very high IC50 value for Aβ aggregation. © 2003 Elsevier Science (USA). All rights reserved.