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Updated: Sep 22, 2025

Non-chromatographic Purification of Recombinant Elastin-like Polypeptides and their Fusions with Peptides and Proteins from Escherichia coli
Published on: June 9, 2014
Quantitative Side-Chain Modifications of Methionine-Containing Elastin-Like Polypeptides as a Versatile Tool to Tune
Jessica R Kramer1, Rosine Petitdemange2,3,4, Laure Bataille2,3,4
1Department of Chemistry and Biochemistry and Department of Bioengineering, University of California, Los Angeles, California 90095, United States.
Abstract:
Tuning the lower critical solution temperature (LCST) of temperature-responsive recombinant elastin-like polypeptides has usually been achieved by designing different protein sequences, in terms of amino acid composition and length, implying tedious molecular cloning steps. In the present work, we have explored the chemoselective alkylation of methionine as an easy means to modify elastin repeat side chains and easily modulate the LCST of the polypeptides. Such a versatile synthetic method shall practically be exploited to modulate any properties of recombinant polymers.

