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

Soft Matter
Edward D H MansfieldSébastien Perrier

Abstract

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.

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Citations

Nov 13, 2018·Macromolecular Rapid Communications·Shuaiyuan HanLaurent Bouteiller
Oct 20, 2018·Chemistry : a European Journal·Huda ShaikhSebastien Perrier
Aug 6, 2020·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Shabnam TarvirdipourCornelia G Palivan
Apr 30, 2020·Chemical Communications : Chem Comm·Franka V GruschwitzJohannes C Brendel
Jul 12, 2019·Chemical Science·Matthias HartliebSébastien Perrier
Oct 19, 2019·Nature Communications·Julia Y RhoSébastien Perrier
May 4, 2021·Chemical Reviews·Qiao SongSébastien Perrier

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Methods Mentioned

BETA
NMR
size exclusion chromatography
amidation
SANS

Software Mentioned

SASfit
SANS
SANS2D

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