Mibel Aguilar1
Monash University1
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 <i>N</i>-acetyl-β<sup>3</sup>-peptides that spontaneously undergo supramolecular self-assembly to form a new class of biomaterials [1-4]. 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. 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. The bioactivity of the resulting materials can be tailored to control cell adherence and function or targeted delivery of bioactive compounds, opening up a new generation of metabolically stable and biocompatible biomaterials [5-7].<br/><br/><b>References</b><br/>1. Del Borgo MP, et al, ‘Supramolecular Self-Assembly of N-Acetyl capped β-Peptides Leads to Nano-to Macroscale Fibre Formation’. <i>Angewandte Chemie Int Ed</i>. 2013, 52 8266-8270.<br/>2. Gopalan R, et al, ‘Geometrically Precise Building Blocks: the Self-Assembly of β-Peptides’, <i>Chemistry & Biology</i>, 22 (2015) 1417-1423.<br/>3. Christofferson AJ, et al, ‘Identifying the Coiled-Coil Triple Helix Structure of β-Peptide Nanofibers at Atomic Resolution.’ ACS Nano, 12 (2018) 9101-9109.<br/>4. 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.<br/>5. Kulkarni K, et l, ‘Sustained release of peptide-based therapeutics from a β3-tripeptide hydrogel through in situ hydrolysis‘, ACS Applied Materials and Interfaces, 13 (2021), 58279-58290.<br/>6, Payne, JAE, Kulkarni K, et al, ‘Staphylococcus aureus entanglement in self-assembling β-peptide nanofibres decorated with vancomycin’, Nanoscale Advances, 3 (2021) 2607-2616.<br/>7. Kulkarni K, et al, ‘Self-Assembly of Trifunctional Tripeptides to Form Neural Scaffolds’, J Materials Chemistry B, 9 (2021) 4475-4479.