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Pharmaceutical Nanotechnology

Editor-in-Chief

ISSN (Print): 2211-7385
ISSN (Online): 2211-7393

Research Article

T-shaped Peptide Amphiphiles Self Assemble into Nanofiber Networks

Author(s): Funmilola A. Fisusi, Rebecca Notman, Louis A. Granger, John P. Malkinson, Andreas G. Schatzlein and Ijeoma F. Uchegbu*

Volume 5, Issue 3, 2017

Page: [215 - 219] Pages: 5

DOI: 10.2174/2211738505666170828095937

Price: $65

Abstract

Background: Conventional nanofiber forming peptide amphiphiles comprise a beta sheet forming, short peptide sequence with an alkyl chain attached at one terminus. We report the selfassembly of a peptide amphiphile possessing a mid-chain located alkyl substituent (a T-shaped peptide amphiphile) into nanofiber networks.

Method: Peptide synthesis was carried out using standard 9-fluorenylmethoxycarbonyl solid phase peptide synthesis protocols, followed by covalent attachment of the alkyl chains to yield target peptide amphiphiles. Self-assembly was then studied using electron microscopy and coarse-grained molecular dynamics simulations.

Results: T-shaped peptide amphiphiles self-assembled into nanofibers just like linear peptide amphiphiles, but then unlike linear peptide amphiphiles, T-shaped peptide amphiphiles formed inter-fiber associations and ultimately nanofiber networks.

Conclusion: Changing the position of the alkyl chain in a peptide amphiphile from the terminal end of the peptide to the middle part of the peptide, to form a T-shaped peptide amphiphile, does not disrupt the molecular interactions required for the self-assembly of the peptide amphiphiles into nanofibers.

Keywords: Beta sheet, drug delivery, molecular dynamics simulations, nanofibers, networks, peptide amphiphiles, peptide synthesis, self-assemblies.

Graphical Abstract


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