Self-assembly in peptides and proteins is an often encountered concept, where constituent building blocks are recruited and stabilized, via carefully orchestrated hydrophobic interactions, hydrogen bonding and other non-covalent interactions, to eventually reveal an array of supramolecular aggregates, with defined structural features. This study presents synthesis and self-assembly of a mannosylated peptide in aqueous medium. Turbidimetric assay with Concanavalin A (Con A), a mannose binding protein, was conducted to confirm the presence of hydrophilic mannose group on the exterior surface of self-assembled structures. DNA encapsulation in these soft structures was achieved by ultrasonication of soft spherical structures in the presence of plasmid DNA. Copyright © 2010 European Peptide Society and John Wiley & Sons, Ltd.