Funmilola A. Fisusi, Rebecca Notman, Louis A. Granger, John P. Malkinson, Andreas G. Schatzlein and Ijeoma F. Uchegbu* Pages 215 - 219 ( 5 )
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.
Beta sheet, drug delivery, molecular dynamics simulations, nanofibers, networks, peptide amphiphiles, peptide synthesis, self-assemblies.
UCL School of Pharmacy, Brunswick Square London, WC1N 1AX, Department of Chemistry and Centre for Scientific Computing, University of Warwick, Coventry, CV4 7AL, Department of Chemistry and Centre for Scientific Computing, University of Warwick, Coventry, CV4 7AL, UCL School of Pharmacy, Brunswick Square London, WC1N 1AX, UCL School of Pharmacy, Brunswick Square London, WC1N 1AX, UCL School of Pharmacy, Brunswick Square London, WC1N 1AX