Nanostructures from the self-assembly of α-helical peptide amphiphiles

Self-assembly of PAs composed of palmitic acid and several repeated heptad peptide sequences, C15H31CO-(IEEYTKK)(n)-NH2 (n=1-4, represented by PA1-PA4), was investigated systematically. The secondary structures of the PAs were characterized by CD. PA3 and PA4 (n=3 and 4, respectively) showed an -helical structure, whereas PA1 and PA2 (n=1 and 2, respectively) did not display an -helical conformations under the tested conditions. The morphology of the self-assembled peptides in aqueous medium was studied by transmission electron microscopy. As the number of heptad repeats in the PAs increased, the nanostructure of the self-assembled peptides changed from nanofibers to nanovesicles. Changes of the secondary structures and the self-assembly morphologies of PA3 and PA4 in aqueous medium with various cations were also studied. The critical micelle concentrations were determined using a pyrene fluorescence probe. In conclusion, this method may be used to design new peptide nanomaterials. Copyright (c) 2014 European Peptide Society and John Wiley & Sons, Ltd.