Cooperative and reciprocal chiral structure formation of an alanine-based peptide confined at the surface of cationic surfactant membranes.

The confinement of anionic oligoalanine peptides at the surface of cationic membranes can cooperatively reinforce peptide/peptide interactions and induce secondary-structure formation, and, reciprocally, induce chirality expression of the membrane at the mesoscopic level, thus leading to the formation of three-dimensional chiral fibrillar networks. Such a strong binding effect of peptides with cationic membranes and the resulting cooperative assembly behaviors are observed with two different types of cationic surfactant, namely, two-head two-tail gemini and one-head two-tail surfactants. The ensemble of assembly properties, such as critical micellar concentration (cmc), Krafft temperature (T(k) ), molecular area at the air/water interface, molecular organization (as studied by FTIR attenuated total reflectance (ATR) measurements and small-angle X-ray scattering), and morphology of the aggregates (as observed by optical and electron microscopy studies), are reported. The results clearly demonstrate that the molecular organization and mesoscopic supramolecular structures are controlled by a subtle balance between the peptide/peptide interactions, ionic interactions between the membranes and peptides, and the interactions the between surfactant molecules, which are governed by hydrophobicity and steric interactions. Investigation into such cooperative organization can shed light on the mechanism of supramolecular chirality expression in membrane systems and allow understanding of the structure of peptides in interactions with lipid bilayers.