PETITDEMANGE, Rosine; GARANGER, Elisabeth; BATAILLE, Laure; BATHANY, Katell; GARBAY, Bertrand; DEMING, Timothy J.; LECOMMANDOUX, Sébastien

doi:10.1021/acs.bioconjchem.7b00082

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PETITDEMANGE, Rosine
Laboratoire de Chimie des Polymères Organiques [LCPO]
Team 3 LCPO : Polymer Self-Assembly & Life Sciences

GARANGER, Elisabeth
Laboratoire de Chimie des Polymères Organiques [LCPO]
Team 3 LCPO : Polymer Self-Assembly & Life Sciences

BATAILLE, Laure
Biologie du fruit et pathologie [BFP]
Laboratoire de Chimie des Polymères Organiques [LCPO]
Team 3 LCPO : Polymer Self-Assembly & Life Sciences

Langue

Article de revue

Ce document a été publié dans

Bioconjugate Chemistry. 2017-04-13, vol. 28, n° 5, p. 1403 - 1412

American Chemical Society

Résumé en anglais

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.< Réduire

Mots clés en anglais

Elastin-like polypeptides

Elastin-like peptide

Post-functionalization modification

DOI

http://dx.doi.org/10.1021/acs.bioconjchem.7b00082

Project ANR

Initiative d'excellence de l'Université de Bordeaux - ANR-10-IDEX-0003

Origine

Importé de hal

Unités de recherche

Biologie du Fruit & Pathologie (BFP) - UMR 1332