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Updated: Aug 5, 2026
Non-chromatographic Purification of Recombinant Elastin-like Polypeptides and their Fusions with Peptides and Proteins from Escherichia coli
Published on: June 9, 2014
Effects of temperature and pressure on the aggregation properties of an engineered elastin model polypeptide in
T Tamura1, T Yamaoka, S Kunugi
1Department of Polymer Science and Engineering, Kyoto Institute of Technology, Matsugasaki, Sakyo, Kyoto 606-8585, Japan.
Abstract:
The pressure and temperature dependence of the cloud point transition of an aqueous solution of an elastin-like polypeptide (MGLDGSMG(VPGIG)40VPLE), prepared by bacterial expression of the corresponding artificial gene, was measured. A temperature-pressure diagram was constructed over a wide range of conditions. The (VPGIG)40 solution exhibited a well-defined pressure-induced cloudpoint (Pc), as well as a temperature-induced transition (Tc). From near atmospheric pressure up to 100 MPa, Tc increased with increasing pressure, but decreased with further increases in pressure above 200 MPa. The maximum Tc was reached at 100-200 MPa. Between 10 and 25 degrees C, the Pc decreased with increasing temperature, and a broad maximum in Pc was observed in the range -10 to 0 degree C. These results are compared with our previous results on synthetic thermoresponsive vinyl polymers.
