Supramolecular Self-Assembly of N-Acetyl-Capped beta-Peptides Leads to Nano-to Macroscale Fiber Formation

M.P. Del Borgo, A.I. Mechler, D. Traore, K.P. Kulkarni, C. Forsyth, J.A. Wilce, M.C.J. Wilce, M.-I. Aguilar, P. Perlmutter
Monash University, AU

Keywords: beta-peptide, supramolecular, self-assembly, fibers

Summary:

14-Helical β3-peptides contain 3 residues per complete turn and thus form cylindrical molecules with perfect longitudinal alignment of residues. This provides extraordinary opportunities for designing new materials with functionality located along these faces. Perhaps even more significant, is that the perfect pitch offers the opportunity to design a supramolecular self-assembly motif to link the monomers in a highly symmetrical manner reminiscent of one dimensional crystallisation. We have now found that 14-helical, N-acetyl β3-peptides spontaneously self-assemble in a unique head-to-tail fashion to form fibres from solution. Fibre size can be controlled from the nano-to macro scale.[1] The inherent flexibility in design and ease of synthesis provide powerful new avenues for the development of novel bio- and nanomaterials via supramolecular self-assembly. Mark P. Del Borgo, Adam I. Mechler, Daouda Traore, Craig Forsyth, Jacqueline A. Wilce, Matthew C. J. Wilce, Marie-Isabel Aguilar, and Patrick Perlmutter, Angew. Chem. Int. Ed. 2013, 52, 8266-8270. Synthesis & application of novel bionanomaterials