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 high symmetry to design lateral supramolecular self-assembly motifs to link the fibres in a controlled manner to form hydrogels with multiple biological cues2,3. The bioactivity of the resulting materials can be tailored to control cell adherence and function, opening up a new generation of metabolically stable and biocompatible biomaterials.
[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