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

Protein Expr Purif. 2016 May:121:81-7. doi: 10.1016/j.pep.2016.01.010. Epub 2016 Jan 21.

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.

Keywords: Elastin-like polypeptides; Mass spectrometry; Precision polymers; Recombinant expression; Transition temperature.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence / genetics
  • Elastin / biosynthesis*
  • Elastin / genetics
  • Escherichia coli / genetics
  • Gene Expression
  • Hydrophobic and Hydrophilic Interactions
  • Peptides / genetics*
  • Recombinant Proteins / biosynthesis*
  • Recombinant Proteins / genetics
  • Transition Temperature

Substances

  • Peptides
  • Recombinant Proteins
  • Elastin