Recent work is replete with examples of beta sheet forming naturally occurring amino acids that assemble into stochastic assemblies such as fibrils, meshes and irregular 3D architectures. While polyethylene glycol (PEG) based linkers have been used to increase the solubility of the beta-sheets, controlling their self-assembly requires better design of the amino acid building block. Here, we report the self-assembly of a non-canonical amino acid based on beta-sheet forming cysteine with a short temperature-responsive ethylene glycol side chain that makes the peptide backbone soluble at the level of the amino acid itself. The polypeptides are synthesized using N-carboxyanhydride ring opening polymerization (NCA-ROP), that enables scalable synthesis of the three-armed polypeptide from a Benzotriazole (BTA) core. Linking the synthetic peptides to a BTA core further enables control of the self-assembly process wherein the BTA core drives the assembly into physical 1D bottlebrushes while the corona peptides pack into parallel beta sheets. The kinetics of self-assembly and resulting morphology is shown to be dependent on peptide length and processing conditions.

Supramolecular bottlebrush-forming non-canonical peptides with benzotriazole (BTA) core for scalable and hierarchical biomaterial self-assembly

ACS Spring 2022

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