Short peptide sequences such as KLVFFAE form well defined beta sheet structures. Their further templating through hydrophobic interactions and hydrogen bonding is the principal determinant of supramolecular organization of Aβ peptides. The aim of this work is to demonstrate that other forces such as electrostatic interactions are likely to play a role as well. Through modification of end blocking groups, we show that different nanostructures could be formed and that the supramolecular organisation of amyloid fibrillar network could be disrupted.