Syracuse

Selective Tuning of Elastin-like Polypeptide Properties via Methionine Oxidation

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Petitdemange, Rosine | Garanger, Elisabeth | Bataille, Laure | Bathany, Katell | Dieryck, Wilfrid | Garbay, Bertrand | Deming, Timothy J. | Lecommandoux, Sébastien

Edité par CCSD ; American Chemical Society -

International audience. We have designed and prepared a recombinant elastin-like polypeptide (ELP) containing precisely positioned methionine residues, and performed the selective and complete oxidation of its methionine thioether groups to both sulfoxide and sulfone derivatives. Since these oxidation reactions substantially increase methionine residue polarity, they were found to be a useful means to precisely adjust the temperature responsive behavior of ELPs in aqueous solutions. In particular, lower critical solution temperatures were found to be elevated in oxidized sample solutions, but were not eliminated. These transition temperatures were found to be further tunable by the use of solvents containing different Hofmeister salts. Overall, the ability to selectively and fully oxidize methionine residues in ELPs proved to be a convenient postmodification strategy for tuning their transition temperatures in aqueous media.

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