Abstract
Statistical copolypeptides comprising lysine and tyrosine with unprecedented ion-induced gelation behavior are reported. Copolypeptides are obtained by one-step N-carboxyanhydride (NCA) ring-opening polymerization. The gelation mechanism is studied by in situ SAXS analyses, in addition to optical spectroscopy and transmission electron microscopy (TEM). It is found that the gelation of these statistically polymerized polypeptides is due to the formation of stable intermolecular β-sheet secondary structures induced by the presence of salt ions as well as the aggregation of an α-helix between the copolypeptides. This behavior is unique to the statistical lysine/tyrosine copolypeptides and was not observed in any other amino acid combination or arrangement. Furthermore, the diffusion and mechanical properties of these hydrogels can be tuned through tailoring the polypeptide chain length and ion strength.
Highlights
Statistical copolypeptides comprising lysine and tyrosine with unprecedented ion-induced gelation behavior are reported
The first is based on the synthesis of peptides with precisely controlled amino acid sequences, of which several examples have been reported to form physical hydrogels either spontaneously or upon a trigger.[10−13] While predominantly oligomeric, these peptides vary in length and share the common feature of forming self-assembled nanostructures through hydrophobic, ionic, hydrogen bonding, or secondary structure interaction.[14−16] These typical higher-order motives include nanotubes, nanotapes, or nanospheres, which aggregate to form hydrogel networks
Three-dimensional networks in aqueous media are formed through hydrophobic, ionic, as well as secondary structure interactions such as β-sheet- or α-helix-driven molecular arrangements.[21]
Summary
Hanay − Department of Chemistry, RCSI University of Medicine and Health Sciences, Dublin 2, Ireland. Kimmins − Instituto de Química, Pontificia Universidad Católica de Valparaíso, Placilla 2950 Valparaíso, Chile. Sally-Ann Cryan − School of Pharmacy and Biomolecular Sciences and Tissue Engineering Research Group, RCSI University of Medicine and Health Sciences, Dublin 2, Ireland; Science Foundation Ireland (SFI) Centre for Research in Medical Devices (CURAM), RCSI, Dublin 2, Ireland; AMBER, The SFI Advanced Materials and Bioengineering Research Centre, RCSI, Dublin 2, Ireland; orcid.org/0000-0002-3941-496X. Daniel Hermida Merino − Dutch-Belgian Beamline (DUBBLE), ESRF - The European Synchrotron Radiation Facility, Grenoble 38043 Cedex 9, France.
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