Recombinant production and purification of short hydrophobic Elastin-like polypeptides with low transition temperatures
BATAILLE, Laure
Institut Européen de Chimie et Biologie [IECB]
Laboratoire de Chimie des Polymères Organiques [LCPO]
Team 3 LCPO : Polymer Self-Assembly & Life Sciences
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Institut Européen de Chimie et Biologie [IECB]
Laboratoire de Chimie des Polymères Organiques [LCPO]
Team 3 LCPO : Polymer Self-Assembly & Life Sciences
BATAILLE, Laure
Institut Européen de Chimie et Biologie [IECB]
Laboratoire de Chimie des Polymères Organiques [LCPO]
Team 3 LCPO : Polymer Self-Assembly & Life Sciences
Institut Européen de Chimie et Biologie [IECB]
Laboratoire de Chimie des Polymères Organiques [LCPO]
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
Laboratoire de Chimie des Polymères Organiques [LCPO]
Team 3 LCPO : Polymer Self-Assembly & Life Sciences
GARANGER, Elisabeth
Institut Européen de Chimie et Biologie [IECB]
Laboratoire de Chimie des Polymères Organiques [LCPO]
Team 3 LCPO : Polymer Self-Assembly & Life Sciences
< Réduire
Institut Européen de Chimie et Biologie [IECB]
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
Protein Expression and Purification. 2016, vol. 121, p. 81-87
Elsevier
Résumé en anglais
Elastin-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 ...Lire la suite >
Elastin-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.< Réduire
Mots clés en anglais
PHASE-TRANSITION
FREE-ENERGY
PROTEIN
EXPRESSION
POLYMERS
NANOPARTICLES
FUSION
Recombinant expression
Transition temperature
Elastin-like polypeptides
Mass spectrometry
Precision polymers
SYSTEM
GENES
MODEL
Origine
Importé de halUnités de recherche