Systematic study of the structural parameters affecting the self-assembly of cyclic peptide-poly(ethylene glycol) conjugates

Edward D.H. Mansfield, Matthias Hartlieb, Sylvain Catrouillet, Julia Y. Rho, Sophie C. Larnaudie, Sarah E. Rogers, Joaquin Sanchis, Johannes C. Brendel, Sébastien Perrier

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17 Citations (Scopus)


Self-assembling cyclic peptides (CP) consisting of amino acids with alternating d- and l-chirality form nanotubes by hydrogen bonding, hydrophobic interactions, and π-π stacking in solution. These highly dynamic materials are emerging as promising supramolecular systems for a wide range of biomedical applications. Herein, we discuss how varying the polymer conformation (linear vs. brush), as well as the number of polymer arms per peptide unimer affects the self-assembly of PEGylated cyclic peptides in different solvents, using small angle neutron scattering. Using the derived information, strong correlations were drawn between the size of the aggregates, solvent polarity, and its ability to compete for hydrogen bonding interactions between the peptide unimers. Using these data, it could be possible to engineer cyclic peptide nanotubes of a controlled length.

Original languageEnglish
Pages (from-to)6320-6326
Number of pages7
JournalSoft Matter
Issue number30
Publication statusPublished - 1 Jan 2018

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