Tuning Thermoresponsive Properties of Cationic Elastin-like Polypeptides by Varying Counterions and Side-Chains.
- Author(s): Petitdemange, Rosine
- Garanger, Elisabeth
- Bataille, Laure
- Bathany, Katell
- Garbay, Bertrand
- Deming, Timothy J
- Lecommandoux, Sébastien
- et al.
Published Web Locationhttps://doi.org/10.1021/acs.bioconjchem.7b00082
We report the synthesis of methionine-containing recombinant elastin-like polypeptides (ELPs) of different lengths that contain periodically spaced methionine residues. These ELPs were chemoselectively alkylated at all methionine residues to give polycationic derivatives. Some of these samples were found to possess solubility transitions in water, where the temperature of these transitions varied with ELP concentration, nature of the methionine alkylating group, and nature of the sulfonium counterions. These studies show that introduction and controlled spacing of methionine sulfonium residues into ELPs can be used as a means both to tune their solubility transition temperatures in water using a variety of different parameters and to introduce new side-chain functionality.