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Updated: Mar 26, 2026
Non-chromatographic Purification of Recombinant Elastin-like Polypeptides and their Fusions with Peptides and Proteins from Escherichia coli
Published on: June 9, 2014
Recombinant production and purification of short hydrophobic Elastin-like polypeptides with low transition
Laure Bataille1, Wilfrid Dieryck2, Agnès Hocquellet2
1University of Bordeaux, LCPO, UMR 5629, F-33600, Pessac, France; CNRS, LCPO, UMR 5629, F-33600, Pessac, France; Bordeaux INP, LCPO, UMR 5629, F-33600, Pessac, France; Institut Européen de Chimie et Biologie, F-33600, Pessac, France.
Abstract:
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 ELPs (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 °C, 12.4 °C and 11.7 °C, respectively.
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