Title

Self-Assembled Nanomaterials Based on Beta (β3) Tetrapeptides

Document Type

Article

Publication Date

4-2016

Publication Details

This article was originally published as:

Seoudi, R. S., Hinds, M. G., Wilson, D. J., Adda, C. G., Del Borgo, M...Mechler, A. (2016). Self-assembled nanomaterials based on beta (β3 ) tetrapeptides. Nanotechnology, 27(13), 1-9. doi: 10.1088/0957-4484/27/13/135606

ISSN: 0957-4484

Abstract

β 3-amino acid based polypeptides offer a unique starting material for the design of self-assembled nanostructures such as fibres and hierarchical dendritic assemblies, due to their well-defined helical geometry in which the peptide side chains align at 120° due to the 3.0–3.1 residue pitch of the helix. In a previous work we have described the head-to-tail self-assembly of N-terminal acetylated β 3-peptides into infinite helical nanorods that was achieved by designing a bioinspired supramolecular self-assembly motif. Here we describe the effect of consecutively more polar side chains on the self-assembly characteristics of β 3-tetrapeptides Ac-β 3Ala-β 3Leu-β 3Ile-β 3Ala (Ac-β3[ALIA]), Ac-β3Ser-β 3Leu-β 3Ile-β 3Ala (Ac-β3[SLIA]) and Ac-β 3Lys-β 3Leu-β 3Ile-β 3Glu (Ac-β3[KLIE]). β 3-tetrapeptides complete 1 1/3 turns of the helix: thus in the oligomeric form the side chain positions shift 120° with each added monomer, forming a regular periodic pattern along the nanorod. Dynamic light scattering (DLS) measurements confirmed that these peptides self-assemble even in highly polar solvents such as water and DMSO, while diffusion-ordered NMR spectroscopy revealed the presence of a substantial monomeric population. Temperature dependence of the size distribution in DLS measurements suggests a dynamic equilibrium between monomers and oligomers. Solution casting produced distinct fibrillar deposits after evaporating the solvent. In the case of the apolar Ac-β 3[ALIA] the longitudinal helix morphology gives rise to geometrically defined (~70°) junctions between fibres, forming a mesh that opens up possibilities for applications e.g. in tissue scaffolding. The deposits of polar Ac-β 3[SLIA] and Ac-β 3[KLIE] exhibit fibres in regular parallel alignment over surface areas in the order of 10 μm.

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David Wilson is affiliated with Avondale College of Higher Education as a Conjoint Senior Lecturer.

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