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

Protein Expression and Purification
Laure BatailleElisabeth Garanger

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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Mar 31, 2015·Protein Expression and Purification·Laure BatailleElisabeth Garanger

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Citations

Nov 5, 2016·Archives of Biochemistry and Biophysics·Dinesh K YadavNarendra Tuteja
Jan 12, 2017·Biomacromolecules·Rosine PetitdemangeSébastien Lecommandoux
Apr 2, 2020·Biointerphases·Markian S BahniukLarry D Unsworth
Oct 4, 2019·Journal of Colloid and Interface Science·L M Bravo-AnayaS Lecommandoux
Apr 7, 2017·Bioconjugate Chemistry·Rosine PetitdemangeSébastien Lecommandoux

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