Abstract
Peptides comprised entirely of β3-amino acids, commonly referred to as β-foldamers, have been shown to self-assemble into a range of materials. Previously, β-foldamers have been functionalised via various side chain chemistries to introduce function to these materials without perturbation of the self-assembly motif. Here, we show that insertion of both rigid and flexible molecules into the backbone structure of the β-foldamer did not disturb the self-assembly, provided that the molecule is positioned between two β3-tripeptides. These hybrid β3-peptide flanked molecules self-assembled into a range of structures. α-Arginlyglycylaspartic acid (RGD), a commonly used cell attachment motif derived from fibronectin in the extracellular matrix, was incorporated into the peptide sequence in order to form a biomimetic scaffold that would support neuronal cell growth. The RGD-containing sequence formed the desired mesh-like scaffold but did not encourage neuronal growth, possibly due to over-stimulation with RGD. Mixing the RGD peptide with a β-foldamer without the RGD sequence produced a well-defined scaffold that successfully encouraged the growth of neurons and enabled neuronal electrical functionality. These results indicate that β3-tripeptides can form distinct self-assembly units separated by a linker and can form fibrous assemblies. The linkers within the peptide sequence can be composed of a bioactive α-peptide and tuned to provide a biocompatible scaffold.
Highlights
The assembly of bioscaffolds using a bottom-up approach offers significant advantages over naturally derived polymer structures, in terms of greater design flexibility
We show that insertion of both rigid and flexible molecules into the backbone structure of the b-foldamer did not disturb the self-assembly, provided that the molecule is positioned between two b3-tripeptides. These hybrid b3-peptide flanked molecules selfassembled into a range of structures. a-Arginlyglycylaspartic acid (RGD), a commonly used cell attachment motif derived from fibronectin in the extracellular matrix, was incorporated into the peptide sequence in order to form a biomimetic scaffold that would support neuronal cell growth
Mixing the RGD peptide with a b-foldamer without the RGD sequence produced a well-defined scaffold that successfully encouraged the growth of neurons and enabled neuronal electrical functionality
Summary
The assembly of bioscaffolds using a bottom-up approach offers significant advantages over naturally derived polymer structures, in terms of greater design flexibility. In particular, can be designed and synthesised to adopt secondary structures, typically b-sheets and ahelices, which self-assemble to give higher order structures.[1–3] Peptide-based self-assembling systems have been used by a number of groups to create a variety of materials for tissue engineering and biomedicine.[3–10]. The main advantages of using peptide self-assembly include the ability to decorate with functional groups at the monomer level and the inherent biocompatibility. Peptides are prone to proteolytic degradation with consequent alterations in the secondary structures which provide the basis for self-assembly. The resulting alteration of sequence or environmental conditions can lead to the loss of the critical self-assembly motif
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