Peptide self-assembled systems offer significant advantages including biological compatibility, ease of synthesis, low toxicity and functionalisability. However, the control over essential features such as chemical, structural and metabolic stability, the scale and relatively slow rate of self-assembly remain significant challenges. We have designed helical N-acetyl-β³-peptides that spontaneously undergo supramolecular self-assembly to form a new class of biomaterials [1-3]. 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 of N-acetyl-β³-peptides, irrespective of amino acid sequence. In addition, the unique helical structure of the peptide monomer offers the opportunity to introduce a wide variety of functions to the new fibres based on straightforward modification of the side chains of the component amino acids. Furthermore, the pitch of the helix is almost exactly three amino acids, resulting in a geometrically defined position of side chain functionalities. These materials are also resistant to proteolytic degradation further adding to their potential as novel biomaterials. 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.
References
1. Del Borgo MP, et al, ‘Supramolecular Self-Assembly of N-Acetyl capped β-Peptides Leads to Nano-to Macroscale Fibre Formation’. Angewandte Chemie Int Ed. 2013, 52 8266-8270.
2. Christofferson AJ, et al, ‘Identifying the Coiled-Coil Triple Helix Structure of β-Peptide Nanofibers at Atomic Resolution.’ ACS Nano, 12 (2018) 9101-9109.
3. Habila N, Kulkarni K, Lee TH, Aguilar MI* and Del Borgo MP*, ‘Multilaminar Nanobelt Architectures Through Self-Assembly of Lipidated β3-Tripeptide Foldamers’. Frontiers in Chemistry, 8: (2020) 217.

Billy Noonan

Appearances