Skip to main content
SpringerLink
Log in

Thermal behaviors of elastin-like polypeptides (ELPs) according to their physical properties and environmental conditions

  • Published:
Biotechnology and Bioprocess Engineering Aims and scope Submit manuscript

Abstract

Elastin-like polypeptides (ELPs) have a distinctive thermal property, transition temperature (Tt), which leads to phase transition. This thermal property depends on the molecular weight (MW) of ELP, ELP concentration, composition of the amino acids constituting ELPs, and ionic strength of the aqueous solution. In order to investigate the effects of ELP length, ionic strength and existence of fusion protein, ELP genes of three different sizes were cloned using the recursive directional ligation (RDL) method and expressed in Escherichia coli. Following purification, thermal behaviors of ELPs were monitored using a spectrophotometer with temperature scanning. The results of our study indicated that Tt shifted to low in accordance with ELP length or increased ionic strength. Additionally, it was observed that Tt was affected by the physical properties of the protein fused with ELPs.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  1. Altman, G. H., F. Diaz, C. Jakuba, T. Calabro, R. L. Horan, J. Chen, H. Lu, J. Richmond, and D. L. Kaplan (2003) Silk-based biomaterials. Biomaterials 24: 401–416.

    Article  CAS  Google Scholar 

  2. Jo, I. H., J. M. Lee, H. Suh, and H. Kim (2007) Bone tissue engineering using marrow stromal cells. Biotechnol. Bioprocess Eng. 12: 48–53.

    Article  CAS  Google Scholar 

  3. Seo, Y. K., H. H. Youn, C. S. Park, K. Y. Song, and J. K. Park (2008) Reinforced bioartificial dermis constructed with collagen threads. Biotechnol. Bioprocess Eng. 13: 745–751.

    Article  CAS  Google Scholar 

  4. Chow, D., M. L. Nunalee, D. W. Lim, A. J. Simnick, and A. Chilkoti (2008) Peptide-based biopolymers in bio-medicine and biotechnology. Mat. Sci. Eng. 62: 125–155.

    Article  Google Scholar 

  5. Meyer, D. E. and A. Chilkoti (2002) Genetically encoded synthesis of protein-based polymers with precisely specified molecular weight and sequence by recursive directional ligation: examples from the elastin-like polypeptide system. Biomacromolecules 3: 357–367.

    Article  CAS  Google Scholar 

  6. Trabbic-Carlson, K., D. E. Meyer, L. Liu, R. Piervincenzi, N. Nath, T. LaBean, and A. Chilkoti (2004) Effect of protein fusion on the transition temperature of an environmentally responsive elastin-like polypepetide: a role for surface hydrophobicity? Protein eng. Des. Sel. 17: 57–66.

    Article  CAS  Google Scholar 

  7. Meyer, D. E. and A. Chilkoti (2002) Protein-Protein Interactions: A Molecular Cloning Manual. 2nd ed., pp. 329–343. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, USA.

    Google Scholar 

  8. Meyer, D. E. and A. Chilkoti (1999) Purification of recombinant proteins by fusion with thermally-responsive polypeptides. Nat. Biotechnol. 17: 1112–1115.

    Article  CAS  Google Scholar 

  9. Meyer, D. E., K. Trabbic-Carlson, and A. Chilkoti (2001) Protein purification by fusion with an environmentally responsive elastin-like polypeptides: effect of polypeptide length on the purification of thioredoxin. Biotechnol. Prog. 17: 720–728.

    Article  CAS  Google Scholar 

  10. Wang, A. A., J. Lee, G. Jenikova, A. Mulchandani, N. V Myung, and W. Chen (2006) Controlled assembly of multi-segment nanowires by histidine-tagged peptides. Nanotechnology 17: 3375–3379.

    Article  CAS  Google Scholar 

  11. Lao, U. L., A. Chen, M. R. Matsumoto, A. Mulchandani, and W. Chen (2007) Cadmium removal from contaminated soil by thermally responsive elastin (ELPEC20) biopolymers. Biotechnol. Bioeng. 98: 349–355.

    Article  CAS  Google Scholar 

  12. Chilkoti, A., M. R. Dreher, D. E. Mayer, and D. Raucher (2002) Targeted drug delivery by thermally responsive polymers. Adv. Drug Deliv. Rev. 54: 613–630.

    Article  CAS  Google Scholar 

  13. Hyun, J. H., W. K. Lee, N. Nath, A. Chilkoti, and S. Zauscher (2004) Capture and release of proteins on the nanoscale by stimuli-responsive elastin-like polypeptide “switches”. J. Am. Chem. Soc. 126: 7330–7335.

    Article  CAS  Google Scholar 

  14. Sambrook, J., E. Fritsch, and T. Maniatis (1989) Molecular Cloning: A Laboratory Manual. 2nd ed., pp. 82–84. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, USA.

    Google Scholar 

  15. Won, J. I., R. J. Meagher, and A. E. Barron (2005) Protein polymer drag-tags for DNA separations by end-labeled free-solution electrophoresis. Electrophoresis 26: 2138–2148.

    Article  CAS  Google Scholar 

  16. Urry, D. W. (1997) Physical chemistry of biological free energy transduction as demonstrated by elastic protein-based polymers. J. Phys. Chem. B. 101: 11007–11028.

    Article  CAS  Google Scholar 

  17. Lim, D. W., K. Trabbic-Carlson, J. A. Mackay, and A. Chilkoti (2007) Improved non-chromatography purification of a recombinant protein by cationic elastin-like polypeptides. Biomacromolecules 8: 1417–1424.

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Chemical Engineering, Hongik University, Seoul, 121-791, Korea

    Ji-Eun Park & Jong-In Won

Authors
  1. Ji-Eun Park
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Jong-In Won
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Jong-In Won.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Park, JE., Won, JI. Thermal behaviors of elastin-like polypeptides (ELPs) according to their physical properties and environmental conditions. Biotechnol Bioproc E 14, 662–667 (2009). https://doi.org/10.1007/s12257-009-0112-1

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s12257-009-0112-1

Keywords

Search

Navigation