Quantitative Side-Chain Modifications of Methionine-Containing Elastin-Like Polypeptides as a Versatile Tool to Tune Their Properties
KRAMER, Jessica R.
Dept of Chemistry and Biochemistry, University of California, Los Angeles [UCLA]
Univ Calif Los Angeles, Dept Bioengn
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Dept of Chemistry and Biochemistry, University of California, Los Angeles [UCLA]
Univ Calif Los Angeles, Dept Bioengn
KRAMER, Jessica R.
Dept of Chemistry and Biochemistry, University of California, Los Angeles [UCLA]
Univ Calif Los Angeles, Dept Bioengn
Dept of Chemistry and Biochemistry, University of California, Los Angeles [UCLA]
Univ Calif Los Angeles, Dept Bioengn
DEMING, Timothy J.
Dept of Chemistry and Biochemistry, University of California, Los Angeles [UCLA]
Univ Calif Los Angeles, Dept Bioengn
Dept of Chemistry and Biochemistry, University of California, Los Angeles [UCLA]
Univ Calif Los Angeles, Dept Bioengn
GARANGER, Elisabeth
Laboratoire de Chimie des Polymères Organiques [LCPO]
Imagerie Moléculaire et Nanobiotechnologies - Institut Européen de Chimie et Biologie [IECB]
Team 3 LCPO : Polymer Self-Assembly & Life Sciences
Laboratoire de Chimie des Polymères Organiques [LCPO]
Imagerie Moléculaire et Nanobiotechnologies - Institut Européen de Chimie et Biologie [IECB]
Team 3 LCPO : Polymer Self-Assembly & Life Sciences
LECOMMANDOUX, Sebastien
Laboratoire de Chimie des Polymères Organiques [LCPO]
Team 3 LCPO : Polymer Self-Assembly & Life Sciences
< Réduire
Laboratoire de Chimie des Polymères Organiques [LCPO]
Team 3 LCPO : Polymer Self-Assembly & Life Sciences
Langue
en
Article de revue
Ce document a été publié dans
ACS Macro Letters. 2015, vol. 4, n° 11, p. 1283-1286
Washington, D.C : American Chemical Society
Résumé en anglais
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 ...Lire la suite >
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.< Réduire
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