Peptide self-assembled systems offer significant advantages including biological compatibility, ease of synthesis, low toxicity and functionalisability. We have designed helical N-acetyl-β3-peptides that spontaneously undergo supramolecular self-assembly to form fibres. The peptide monomers self-assemble in a unique head-to-tail fashion which is driven by a 3-point H-bond motif associated with the 14-helical structure that is unique to N-acetyl-β3-peptides1. In addition, the helical structure of the peptide monomer, irrespective of amino acid sequence, offers the opportunity to introduce a wide variety of functions to the new fibres based on relatively simple modification of the side chains of the component amino acids. Furthermore, we have developed a number of novel amino acids to introduce greater functionality within these monomers without perturbation of the self-assembly. These materials are also resistant to proteolytic degradation further adding to their potential as novel biomaterials.
We have exploited this 14-helical structure to introduce lateral supramolecular self-assembly motifs to grow fibres in a controlled manner to form hydrogels with multiple biological cues2,3. The use of orthogonal protecting strategies on solid support to synthesise materials that can be tailored to control function will be discussed.
1 Del Borgo, M.P. Angew. Chem. Int. Ed. 2013, 52, 8266-8270. Supramolecular Self‐Assembly of N‐Acetyl‐Capped β‐Peptides Leads to Nano‐to Macroscale Fiber Formation
2 Motamed, S. Soft Matter 2016, 12, 2243-2246. A self-assembling β-peptide hydrogel for neural tissue engineering
3 Kulkarni, K. Chem. Commun.. 2016, 52, 5844-5847. Orthogonal strategy for the synthesis of dual-functionalised β 3-peptide based hydrogels