Non-chromatographic purification of recombinant elastin-like polypeptides and their fusions with peptides and proteins from Escherichia coli

Journal of Visualized Experiments

Volumn , Issue 88, 2014, Pages

  MacEwan, Sarah R ^a,b   Hassouneh, Wafa ^a,b   Chilkoti, Ashutosh ^a,b  

^a Duke University   (United States)

^b DUKE UNIVERSITY   (United States)

Author keywords

Batch purification; Elastin like polypeptides; Inverse transition cycling; Issue 88; Lower critical solution temperature; Molecular Biology; Phase separation; Protein purification

Indexed keywords

EID: 84902156819     PISSN: 1940087X     EISSN: None     Source Type: Journal    
DOI: 10.3791/51583     Document Type: Article

References (29)

1. Urry, D. W. Physical Chemistry of Biological Free Energy Transduction As Demonstrated by Elastic Protein-Based Polymers. J. Phys. Chem. B. 101, 11007-11028, doi:10.1021/jp972167 (1997).
2. Sallach, R. E., Conticello, V. P., & Chaikof, E. L. Expression of a recombinant elastin-like protein in pichia pastoris. Biotechnology progress. 25, 1810-1818, doi:10.1002/btpr.208 (2009).
3. Schipperus, R., Teeuwen, R. L., Werten, M. W., Eggink, G., & de Wolf, F. A. Secreted production of an elastin-like polypeptide by Pichia pastoris. Appl Microbiol Biotechnol. 85, 293-301, doi:10.1007/s00253-009-2082-9 (2009).
4. Schipperus, R., Eggink, G., & de Wolf, F. A. Secretion of elastin-like polypeptides with different transition temperatures by Pichia pastoris. Biotechnology progress. 28, 242-247, doi:10.1002/btpr.717 (2012).
5. Herzog, R. W., Singh, N. K., Urry, D. W., & Daniell, H. Expression of a synthetic protein-based polymer (elastomer) gene in Aspergillus nidulans. Appl Microbiol Biotechnol. 47, 368-372, doi:10.1007/s002530050942 (1997).
6. Conley, A. J., Joensuu, J. J., Jevnikar, A. M., Menassa, R., & Brandle, J. E. Optimization of elastin-like polypeptide fusions for expression and purification of recombinant proteins in plants. Biotechnology and bioengineering. 103, 562-573, doi:10.1002/bit.22278 (2009).
7. Conrad, U. et al. ELPylated anti-human TNF therapeutic single-domain antibodies for prevention of lethal septic shock. Plant biotechnology journal. 9, 22-31, doi:10.1111/j.1467-7652.2010.00523.x (2011).
8. Kaldis, A. et al. High-level production of human interleukin-10 fusions in tobacco cell suspension cultures. Plant biotechnology journal. 11, 535-545, doi:10.1111/pbi.12041 (2013).
9. Meyer, D. E., & Chilkoti, A. 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, doi:10.1021/bm015630n (2002).
10. McDaniel, J. R., Mackay, J. A., Quiroz, F. G., & Chilkoti, A. Recursive directional ligation by plasmid reconstruction allows rapid and seamless cloning of oligomeric genes. Biomacromolecules. 11, 944-952, doi:10.1021/bm901387t (2010).
11. Amiram, M., Quiroz, F. G., Callahan, D. J., & Chilkoti, A. A highly parallel method for synthesizing DNA repeats enables the discovery of 'smart' protein polymers. Nat Mater. 10, 141-148, doi:10.1038/nmat2942 (2011).
12. Meyer, D. E., & Chilkoti, A. Quantification of the effects of chain length and concentration on the thermal behavior of elastin-like polypeptides. Biomacromolecules. 5, 846-851, doi:10.1021/bm034215n (2004).
13. Urry, D. W. et al. Temperature of Polypeptide Inverse Temperature Transition Depends on Mean Residue Hydrophobicity. Journal of the American Chemical Society. 113, 4346-4348, doi:10.1021/Ja00011a057 (1991).
14. Urry, D. W. The change in Gibbs free energy for hydrophobic association-Derivation and evaluation by means of inverse temperature transitions. Chem Phys Lett. 399, 177-183, doi:10.1016/J.Cplett.2004.09.137 (2004).
15. Cho, Y. et al. Effects of Hofmeister anions on the phase transition temperature of elastin-like polypeptides. The journal of physical chemistry. B. 112, 13765-13771, doi:10.1021/jp8062977 (2008).
16. Kim, B., & Chilkoti, A. Allosteric actuation of inverse phase transition of a stimulus-responsive fusion polypeptide by ligand binding. J Am Chem Soc. 130, 17867-17873, doi:10.1021/ja8059057 (2008).
17. Hassouneh, W., Nunalee, M. L., Shelton, M. C., & Chilkoti, A. Calcium binding peptide motifs from calmodulin confer divalent ion selectivity to elastin-like polypeptides. Biomacromolecules. 14, 2347-2353, doi:10.1021/bm400464s (2013).
18. Nettles, D. L., Chilkoti, A., & Setton, L. A. Applications of elastin-like polypeptides in tissue engineering. Adv Drug Deliv Rev. 62, 1479-1485, doi:10.1016/j.addr.2010.04.002 (2010).
19. MacEwan, S. R., & Chilkoti, A. Elastin-like polypeptides: biomedical applications of tunable biopolymers. Biopolymers. 94, 60-77, doi:10.1002/bip.21327 (2010).
20. McDaniel, J. R., Callahan, D. J., & Chilkoti, A. Drug delivery to solid tumors by elastin-like polypeptides. Adv Drug Deliv Rev. 62, 1456-1467, doi:10.1016/j.addr.2010.05.004 (2010).
21. Hassouneh, W., Christensen, T., & Chilkoti, A. Elastin-like polypeptides as a purification tag for recombinant proteins. Curr Protoc Protein Sci. Chapter 6, Unit 6.11, doi:10.1002/0471140864.ps0611s61 (2010).
22. Shamji, M. F. et al. Development and characterization of a fusion protein between thermally responsive elastin-like polypeptide and interleukin-1 receptor antagonist: sustained release of a local antiinflammatory therapeutic. Arthritis Rheum. 56, 3650-3661, doi:10.1002/art.22952 (2007).
23. Hassouneh, W. et al. Unexpected multivalent display of proteins by temperature triggered self-assembly of elastin-like polypeptide block copolymers. Biomacromolecules. 13, 1598-1605, doi:10.1021/bm300321n (2012).
24. Lan, D. M. et al. An improved nonchromatographic method for the purification of recombinant proteins using elastin-like polypeptide-tagged proteases. Analytical Biochemistry. 415, 200-202, doi:10.1016/J.Ab.2011.04.034 (2011).
25. Bellucci, J. J., Amiram, M., Bhattacharyya, J., McCafferty, D., & Chilkoti, A. Three-in-one chromatography-free purification, tag removal, and site-specific modification of recombinant fusion proteins using sortase A and elastin-like polypeptides. Angewandte Chemie. 52, 3703-3708, doi:10.1002/anie.201208292 (2013).
26. Compton, S. J., & Jones, C. G. Mechanism of dye response and interference in the Bradford protein assay. Anal Biochem. 151, 369-374, doi:10.1016/0003-2697(85)90190-3 (1985).
27. McPherson, D. T., Xu, J., & Urry, D. W. Product purification by reversible phase transition followingEscherichia coli expression of genes encoding up to 251 repeats of the elastomeric pentapeptide GVGVP. Protein expression and purification. 7, 51-57, doi:10.1006/prep.1996.0008 (1996).
28. Meyer, D. E., & Chilkoti, A. Purification of recombinant proteins by fusion with thermally-responsive polypeptides. Nat Biotechnol. 17, 1112-1115, doi:10.1038/15100 (1999).
29. McDaniel, J. R. et al. Self-assembly of thermally responsive nanoparticles of a genetically encoded peptide polymer by drug conjugation. Angewandte Chemie. 52, 1683-1687, doi:10.1002/anie.201200899 (2013).