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

• Three hydrophobic ELPs (VPGIG)n with n = 20,40 and 60 were expressed in E. coli.
• The recombinant ELPs were purified to homogeneity.
• Their exact molecular weight was confirmed by mass spectrometry analyzes.
• Transition temperatures in low salt buffer ranged between 11.7°c and 18.6 °C.

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.