aDipartimento Farmaco-chimico, Università degli Studi di Bari, Via Orabona 4, 70125 Bari, Italy
bDipartimento Geomineralogico, Università degli Studi di Bari, Via Orabona 4, 70125 Bari, Italy
Abstract:
A series of N-terminus benzamides of glycine-based symmetric peptides, linked to m-xylylenediamine and 3,4′-oxydianiline spacers, were prepared and tested as inhibitors of β-amyloid peptide Aβ1–40 aggregation in vitro. Compounds with good anti-aggregating activity were detected. Polyphenolic amides showed the highest anti-aggregating activity, with IC50 values in the micromolar range. Structure–activity relationships suggested that π–π stacking and hydrogen-bonding interactions play a key role in the inhibition of Aβ1–40 self-assembly leading to amyloid fibrils.