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Recombinant production and purification of short hydrophobic Elastin-like polypeptides with low transition temperatures

dc.rights.licenseopen
hal.structure.identifierInstitut Européen de Chimie et Biologie [IECB]
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.identifierBiotechnologie des protéines recombinantes à visée santé
dc.contributor.authorDIERYCK, Wilfried
hal.structure.identifierBiotechnologie des protéines recombinantes à visée santé
dc.contributor.authorHOCQUELLET, Agnès
hal.structure.identifierBiotechnologie des protéines recombinantes à visée santé
dc.contributor.authorCABANNE, Charlotte
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.authorLECOMMANDOUX, Sebastien
hal.structure.identifierBiotechnologie des protéines recombinantes à visée santé
dc.contributor.authorGARBAY, Bertrand
IDREF: 033777551
hal.structure.identifierInstitut Européen de Chimie et Biologie [IECB]
hal.structure.identifierLaboratoire de Chimie des Polymères Organiques [LCPO]
hal.structure.identifierTeam 3 LCPO : Polymer Self-Assembly & Life Sciences
dc.contributor.authorGARANGER, Elisabeth
IDREF: 089451740
dc.date.accessioned2020
dc.date.available2020
dc.date.issued2016
dc.identifier.issn1046-5928
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/20277
dc.description.abstractEnElastin-like polypeptides (ELPs) are biodegradable polymers with interesting physico-chemical properties for biomedical and biotechnological applications. We report herein the recombinant expression of three hydrophobic ELP5 (VPGIG)(n) with variable lengths (n = 20, 40, 60) and sub-ambient transition temperatures. These ELPs were purified from the cytoplasmic soluble fraction of Escherichia coli by inverse transition cycling, and their exact molecular weight was confirmed by various mass spectrometry techniques. Transition temperatures of ELP20, ELP40, and ELP60 were measured at 18.6 degrees C, 12.4 degrees C and 11.7 degrees C, respectively.
dc.language.isoen
dc.publisherElsevier
dc.subject.enPHASE-TRANSITION
dc.subject.enFREE-ENERGY
dc.subject.enPROTEIN
dc.subject.enEXPRESSION
dc.subject.enPOLYMERS
dc.subject.enNANOPARTICLES
dc.subject.enFUSION
dc.subject.enRecombinant expression
dc.subject.enTransition temperature
dc.subject.enElastin-like polypeptides
dc.subject.enMass spectrometry
dc.subject.enPrecision polymers
dc.subject.enSYSTEM
dc.subject.enGENES
dc.subject.enMODEL
dc.title.enRecombinant production and purification of short hydrophobic Elastin-like polypeptides with low transition temperatures
dc.typeArticle de revue
dc.identifier.doi10.1016/j.pep.2016.01.010
dc.subject.halChimie/Polymères
bordeaux.journalProtein Expression and Purification
bordeaux.page81-87
bordeaux.volume121
bordeaux.hal.laboratoriesLaboratoire de Chimie des Polymères Organiques (LCPO) - UMR 5629*
bordeaux.institutionBordeaux INP
bordeaux.institutionUniversité de Bordeaux
bordeaux.peerReviewedoui
hal.identifierhal-01360540
hal.version1
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-01360540v1
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Protein%20Expression%20and%20Purification&rft.date=2016&rft.volume=121&rft.spage=81-87&rft.epage=81-87&rft.eissn=1046-5928&rft.issn=1046-5928&rft.au=BATAILLE,%20Laure&DIERYCK,%20Wilfried&HOCQUELLET,%20Agn%C3%A8s&CABANNE,%20Charlotte&BATHANY,%20Katell&rft.genre=article


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