Using protein folding motifs to generate complex, hierarchically-organized micellar structures

POLY 249

Harm-Anton Klok, harm-anton.klok@epfl.ch, Guido WM. Vandermeulen, and Harald Nuhn. Institut des Materiaux, Laboratoire des Polymeres, Ecole Polytechnique Federale de Lausanne, Batiment MX-D, 1015 Lausanne, Switzerland
This contribution discusses the use of biologically-inspired peptide sequences as auxiliaries to mediate self-assembly of synthetic macromolecules into hierarchically-organized solution nanostructures. Peptide sequences inspired by the coiled coil motif and “switch” peptides, which can adopt both amphiphilic β-strand conformations as well as α-helical secondary structures, were conjugated to poly(ethylene glycol) (PEG). The aqueous solution self-assembly of these hybrid block copolymers was investigated using a variety of spectroscopic, scattering and microscopic techniques. These experiments revealed that the folding and organization properties of the peptide sequences are retained upon conjugation of PEG and that they provide the driving force for the formation of the different nanoscale structures which were observed. The possibility of using defined peptide sequences to direct structure formation of synthetic polymers together with the potential of peptide sequences to induce a specific biological response offers interesting prospects for the development of novel self-assembled and biologically active materials.