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

Laure Bataille (1, 2, 3) , Wilfried Dieryck (4) , Agnès Hocquellet (4) , Charlotte Cabanne (4) , Katell Bathany (5) , Sébastien Lecommandoux (2, 3) , Bertrand Garbay (4) , Elisabeth Garanger (1, 2, 3)

1 IECB - Institut Européen de Chimie et Biologie
2 LCPO - Laboratoire de Chimie des Polymères Organiques
3 Team 3 LCPO : Polymer Self-Assembly & Life Sciences
4 Biotechnologie des protéines recombinantes à visée santé
5 CBMN - Chimie et Biologie des Membranes et des Nanoobjets

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.

Mots clés: Elastin-like polypeptides; Mass spectrometry; Precision polymers; Recombinant expression; Transition temperature; PHASE-TRANSITION; FREE-ENERGY; PROTEIN; EXPRESSION; POLYMERS; NANOPARTICLES; FUSION; SYSTEM; GENES; MODEL

Domaines: Polymères

Laure Bataille, Wilfried Dieryck, Agnès Hocquellet, Charlotte Cabanne, Katell Bathany, et al.. Recombinant production and purification of short hydrophobic Elastin-like polypeptides with low transition temperatures. Protein Expression and Purification, 2016, 121, pp.81-87. ⟨10.1016/j.pep.2016.01.010⟩. ⟨hal-01360540⟩