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hal.structure.identifierLaboratoire de Chimie des Polymères Organiques [LCPO]
hal.structure.identifierTeam 3 LCPO : Polymer Self-Assembly & Life Sciences
dc.contributor.authorPETITDEMANGE, Rosine
hal.structure.identifierLaboratoire de Chimie des Polymères Organiques [LCPO]
hal.structure.identifierTeam 3 LCPO : Polymer Self-Assembly & Life Sciences
dc.contributor.authorGARANGER, Elisabeth
hal.structure.identifierBiologie du fruit et pathologie [BFP]
hal.structure.identifierLaboratoire de Chimie des Polymères Organiques [LCPO]
hal.structure.identifierTeam 3 LCPO : Polymer Self-Assembly & Life Sciences
dc.contributor.authorBATAILLE, Laure
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorBATHANY, Katell
hal.structure.identifierLaboratoire de Chimie des Polymères Organiques [LCPO]
hal.structure.identifierTeam 3 LCPO : Polymer Self-Assembly & Life Sciences
dc.contributor.authorGARBAY, Bertrand
hal.structure.identifierUniv Calif Los Angeles, Dept Bioengn
hal.structure.identifierDept of Chemistry and Biochemistry, University of California, Los Angeles [UCLA]
dc.contributor.authorDEMING, Timothy J.
hal.structure.identifierLaboratoire de Chimie des Polymères Organiques [LCPO]
hal.structure.identifierTeam 3 LCPO : Polymer Self-Assembly & Life Sciences
dc.contributor.authorLECOMMANDOUX, Sébastien
dc.date.issued2017-04-13
dc.identifier.issn1043-1802
dc.description.abstractEnWe 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.
dc.language.isoen
dc.publisherAmerican Chemical Society
dc.subject.enElastin-like polypeptides
dc.subject.enElastin-like peptide
dc.subject.enPost-functionalization modification
dc.title.enTuning Thermoresponsive Properties of Cationic Elastin-like Polypeptides by Varying Counterions and Side-Chains
dc.typeArticle de revue
dc.identifier.doi10.1021/acs.bioconjchem.7b00082
dc.subject.halChimie/Matériaux
dc.subject.halChimie/Polymères
dc.subject.halPhysique [physics]/Matière Condensée [cond-mat]/Matière Molle [cond-mat.soft]
dc.subject.halSciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire/Biologie moléculaire
bordeaux.journalBioconjugate Chemistry
bordeaux.page1403 - 1412
bordeaux.volume28
bordeaux.issue5
bordeaux.peerReviewedoui
hal.identifierhal-01646801
hal.version1
hal.popularnon
hal.audienceInternationale
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-01646801v1
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Bioconjugate%20Chemistry&rft.date=2017-04-13&rft.volume=28&rft.issue=5&rft.spage=1403%20-%201412&rft.epage=1403%20-%201412&rft.eissn=1043-1802&rft.issn=1043-1802&rft.au=PETITDEMANGE,%20Rosine&GARANGER,%20Elisabeth&BATAILLE,%20Laure&BATHANY,%20Katell&GARBAY,%20Bertrand&rft.genre=article


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