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Self-Assembled Nanomaterials Based on Beta (β3) Tetrapeptides

avondale-bepress.context-key9759142
avondale-bepress.submission-pathsci_math_papers/83
avondale.facultyScience
avondale.reporting.isPeerReviewedPeer Reviewed
avondale.reporting.versionPublished Version
dc.contributor.authorMechler, Adam
dc.contributor.authorPerimutter, Patrick
dc.contributor.authorAguilar, Marie-Isabel
dc.contributor.authorDel Borgo, Mark
dc.contributor.authorAdda, Christopher G.
dc.contributor.authorWilson, David J.
dc.contributor.authorHinds, Mark G.
dc.contributor.authorSeoudi, Rania S.
dc.date.accessioned2023-11-01T00:24:42Z
dc.date.available2023-11-01T00:24:42Z
dc.date.issued2016-04-01
dc.date.submitted2017-02-27T21:22:17Z
dc.description.abstract<p><em>β</em> 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 <em>β</em> 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 <em>β</em> 3-tetrapeptides Ac-<em>β</em> 3Ala-<em>β</em> 3Leu-<em>β</em> 3Ile-<em>β</em> 3Ala (Ac-β3[ALIA]), Ac-<em>β</em>3Ser-<em>β</em> 3Leu-<em>β</em> 3Ile-<em>β</em> 3Ala (Ac-β3[SLIA]) and Ac-<em>β</em> 3Lys-<em>β</em> 3Leu-<em>β</em> 3Ile-<em>β</em> 3Glu (Ac-β3[KLIE]). <em>β</em> 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-<em>β</em> 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-<em>β</em> 3[SLIA] and Ac-<em>β</em> 3[KLIE] exhibit fibres in regular parallel alignment over surface areas in the order of 10 <em>μ</em>m.</p>
dc.identifier.citation<p>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. <em>Nanotechnology, 27</em>(13), 135606. doi:10.1088/0957-4484/27/13/135606</p>
dc.identifier.doihttps://doi.org/10.1088/0957-4484/27/13/135606
dc.identifier.issn1361-6528
dc.identifier.urihttps://research.avondale.edu.au/handle/1897/09759142
dc.language.isoen_us
dc.provenance<p>This article was originally published as:</p> <p>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. <em>Nanotechnology, 27</em>(13), 1-9. doi: 10.1088/0957-4484/27/13/135606</p> <p>ISSN: 0957-4484</p>
dc.relation.ispartofNanotechnology
dc.rights<p>Due to copyright restrictions this article is unavailable for download.</p> <p>Copyright © 2016 IOP Publishing Ltd</p>
dc.subjectbioinspired fibrous materials
dc.subjectsupramolecular self-assembly
dc.subjectatomic force microscopy
dc.subjectbottom-up nanofabrication
dc.titleSelf-Assembled Nanomaterials Based on Beta (β3) Tetrapeptides
dc.typeJournal Article

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