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Issue 24, 2017
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Balancing the intermolecular forces in peptide amphiphiles for controlling self-assembly transitions

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Abstract

While the influence of alkyl chain length and headgroup size on self-assembly behaviour has been well-established for simple surfactants, the rational control over the pH- and concentration-dependent self-assembly behaviour in stimuli responsive peptides remains an elusive goal. Here, we show that different amphiphilic peptides can have similar self-assembly phase diagrams, providing the relative strengths of the attractive and repulsive forces are balanced. Using palmitoyl-YYAAEEEEK(DO3A:Gd)-NH2 and palmitoyl-YAAEEEEK(DO3A:Gd)-NH2 as controls, we show that reducing hydrophobic attractive forces through fewer methylene groups in the alkyl chain will lead to a similar self-assembly phase diagram as increasing the electrostatic repulsive forces via the addition of a glutamic acid residue. These changes allow creation of self-assembled MRI vehicles with slightly different micelle and nanofiber diameters but with minimal changes in the spin–lattice T1 relaxivity. These findings reveal a powerful strategy to design self-assembled vehicles with different sizes but with similar self-assembly profiles.

Graphical abstract: Balancing the intermolecular forces in peptide amphiphiles for controlling self-assembly transitions

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Publication details

The article was received on 07 Apr 2017, accepted on 29 May 2017 and first published on 30 May 2017


Article type: Paper
DOI: 10.1039/C7OB00875A
Citation: Org. Biomol. Chem., 2017,15, 5220-5226
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    Balancing the intermolecular forces in peptide amphiphiles for controlling self-assembly transitions

    C. J. Buettner, A. J. Wallace, S. Ok, A. A. Manos, M. J. Nicholl, A. Ghosh, M. F. Tweedle and J. E. Goldberger, Org. Biomol. Chem., 2017, 15, 5220
    DOI: 10.1039/C7OB00875A

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