Supramolecular self-assembly of N-acetyl Beta3-peptide amphiphiles
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1
Monash University, Biochemistry and Molecular Biology, Australia
Self-assembly (SA) of peptides provides a flexible approach to developing novel materials with tailored morphologies and desired functions by modulating design and engineering of monomers[1]-[3]. Natural amino acids have been frequently utilized in the design of sequences. Although promising, they still have some draw backs in terms of structural and metabolic stability as well as ease of functionalization[4]. Using peptides consisting of only β-amino acids offers the means to overcome these limitations. Recently, our group reported that N-terminal acetylated β3-peptides can self-assemble by head-to-tail into helical fibrils through a supramolecular three point H-bonding motif[5]. We have also tuned the self-assembly of β3-peptides to present a range of morphologies by the appropriate solvent medium[6]. In order to further understand the control of self-assembly and engineer new architectures, here we show a new class of β3-peptide amphiphiles consisting of alkyl chains of either C12, C14 or C16 that can self-assemble in a unique pattern. Self-assembly was investigated using atomic force microscopy and transmission electron microscopy. The alkyl chain was attached at different positions and β3-peptide amphiphiles with identical composition but with a different sequence arrangement and position of alkyl chain self-assembled into different types of nanostructures under the same conditions. We found that β3-peptide amphiphiles with the alkyl chain on the N-terminus or residue 1 self-assembled into twisted fibrous nanostructures. By comparison, when the alkyl chain is located at residue 2 or 3, self-assembly resulted in flat nanobelts. The results clearly demonstrate the significance of the position of an alkyl chain on the peptide backbone sequence in determining supramolecular architectures. These outcomes will give further insight into the design and control of β3-peptide amphiphile self-assembly.
References:
[1] Aida, T., E.W. Meijer, and S.I. Stupp, Functional supramolecular polymers. Science, 2012. 335(6070): p. 813-817
[2] Woolfson, D.N. and Z.N. Mahmoud, More than just bare scaffolds: towards multi-component and decorated fibrous biomaterials. Chemical Society Reviews, 2010. 39(9): p. 3464-3479
[3] Tsutsumi, H. and H. Mihara, Soft materials based on designed self-assembling peptides: From design to application. Molecular BioSystems, 2013. 9(4): p. 609-617
[4] Woolfson, D.N. and M.G. Ryadnov, Peptide-based fibrous biomaterials: some things old, new and borrowed. Current Opinion in Chemical Biology, 2006. 10(6): p. 559-567
[5] Del Borgo, M.P., et al., Supramolecular self-assembly of N-acetyl-capped β-peptides leads to nano- to macroscale fiber formation. Angewandte Chemie - International Edition, 2013. 52(32): p. 8266-8270
[6] Seoudi, R.S., et al., Supramolecular self-assembly of 14-helical nanorods with tunable linear and dendritic hierarchical morphologies. New Journal of Chemistry, 2015
Keywords:
self-assembly,
nanofiber,
amphiphile
Conference:
10th World Biomaterials Congress, Montréal, Canada, 17 May - 22 May, 2016.
Presentation Type:
Poster
Topic:
Nano-structured materials for unique functions
Citation:
Habila
N,
Kulkarni
KP,
Lee
T,
Del Borgo
MP and
Aguilar
MI
(2016). Supramolecular self-assembly of N-acetyl Beta3-peptide amphiphiles.
Front. Bioeng. Biotechnol.
Conference Abstract:
10th World Biomaterials Congress.
doi: 10.3389/conf.FBIOE.2016.01.02516
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Received:
27 Mar 2016;
Published Online:
30 Mar 2016.