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Sequence heuristics to encode phase behaviour in intrinsically disordered protein polymers

Quiroz, Felipe García, Chilkoti, Ashutosh·2015·Nature Materials

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  1. Li, P. et al. Phase transitions in the assembly of multivalent signalling proteins. Nature 483, 336–340 (2012). · DOI
  2. Weber, S. C. & Brangwynne, C. P. Getting RNA and protein in phase. Cell 149, 1188–1191 (2012). · DOI
  3. Vekilov, P. G. Phase transitions of folded proteins. Soft Matter 6, 5254–5272 (2010). · DOI
  4. Toretsky, J. A. & Wright, P. E. Assemblages: Functional units formed by cellular phase separation. J. Cell Biol. 206, 579–588 (2014). · DOI
  5. Frey, S., Richter, R. P. & Görlich, D. FG-rich repeats of nuclear pore proteins form a three-dimensional meshwork with hydrogel-like properties. Science 314, 815–817 (2006). · DOI
  6. Stuart, M. A. C. et al. Emerging applications of stimuli-responsive polymer materials. Nature Mater. 9, 101–113 (2010). · DOI
  7. McDaniel, J. R. et al. Self-assembly of thermally responsive nanoparticles of a genetically encoded peptide polymer by drug conjugation. Angew. Chem. Int. Ed. 52, 1683–1687 (2013). · DOI
  8. MacKay, J. A. et al. Self-assembling chimeric polypeptide–doxorubicin conjugate nanoparticles that abolish tumours after a single injection. Nature Mater. 8, 993–999 (2009). · DOI · Paper page
  9. Liu, W. et al. Brachytherapy using injectable seeds that are self-assembled from genetically encoded polypeptides in situ. Cancer Res. 72, 5956–5965 (2012). · DOI
  10. Nishida, K. et al. Corneal reconstruction with tissue-engineered cell sheets composed of autologous oral mucosal epithelium. New Eng. J. Med. 351, 1187–1196 (2004). · DOI
  11. Koria, P. et al. Self-assembling elastin-like peptides growth factor chimeric nanoparticles for the treatment of chronic wounds. Proc. Natl Acad. Sci. USA 108, 1034–1039 (2011). · DOI
  12. Meyer, D. E. & Chilkoti, A. Purification of recombinant proteins by fusion with thermally-responsive polypeptides. Nature Biotechnol. 17, 1112–1115 (1999). · DOI
  13. 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. Angew. Chem. Int. Ed. 52, 3703–3708 (2013). · DOI
  14. Stayton, P. S. et al. Control of protein–ligand recognition using a stimuli-responsive polymer. Nature 378, 472–474 (1995). · DOI
  15. Habchi, J., Tompa, P., Longhi, S. & Uversky, V. N. Introducing protein intrinsic disorder. Chem. Rev. 114, 6561–6588 (2014). · DOI
  16. Li, N. K., Quiroz, F. G., Hall, C. K., Chilkoti, A. & Yingling, Y. G. Molecular description of the LCST behaviour of an elastin-like polypeptide. Biomacromolecules 15, 3522–3530 (2014). · DOI
  17. Muiznieks, L. D. & Keeley, F. W. Proline periodicity modulates the self-assembly properties of elastin-like polypeptides. J. Biol. Chem. 285, 39779–39789 (2010). · DOI
  18. Dutta, N. K. et al. A genetically engineered protein responsive to multiple stimuli. Angew. Chem. Int. Ed. 50, 4428–4431 (2011). · DOI
  19. Rauscher, S., Baud, S., Miao, M., Keeley, F. W. & Pomès, R. Proline and glycine control protein self-organization into elastomeric or amyloid fibrils. Structure 14, 1667–1676 (2006). · DOI
  20. De Las Heras Alarcon, C., Pennadam, S. & Alexander, C. Stimuli responsive polymers for biomedical applications. Chem. Soc. Rev. 34, 276–285 (2005). · DOI
  21. 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. Nature Mater. 10, 141–148 (2011). · DOI
  22. Balu, R. et al. An16-resilin: An advanced multi-stimuli-responsive resilin-mimetic protein polymer. Acta Biomater. 10, 4768–4777 (2014). · DOI
  23. Urry, D. W. et al. Hydrophobicity scale for proteins based on inverse temperature transitions. Biopolymers 32, 1243–1250 (1992). · DOI
  24. Das, R. K. & Pappu, R. V. Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues. Proc. Natl Acad. Sci. USA 110, 13392–13397 (2013). · DOI
  25. Yokoi, H., Kinoshita, T. & Zhang, S. Dynamic reassembly of peptide RADA16 nanofiber scaffold. Proc. Natl Acad. Sci. USA 102, 8414–8419 (2005). · DOI
  26. Müller-Späth, S. et al. Charge interactions can dominate the dimensions of intrinsically disordered proteins. Proc. Natl Acad. Sci. USA 107, 14609–14614 (2010). · DOI
  27. Möglich, A., Joder, K. & Kiefhaber, T. End-to-end distance distributions and intrachain diffusion constants in unfolded polypeptide chains indicate intramolecular hydrogen bond formation. Proc. Natl Acad. Sci. USA 103, 12394–12399 (2006). · DOI
  28. 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 (2002). · DOI · Paper page
  29. Seuring, J. & Agarwal, S. First example of a universal and cost-effective approach: Polymers with tunable upper critical solution temperature in water and electrolyte solution. Macromolecules 45, 3910–3918 (2012). · DOI
  30. Shimada, N. et al. Ureido-derivatized polymers based on both poly (allylurea) and poly (L-citrulline) exhibit UCST-type phase transition behaviour under physiologically relevant conditions. Biomacromolecules 12, 3418–3422 (2011). · DOI
  31. Seuring, J. & Agarwal, S. Polymers with upper critical solution temperature in aqueous solution: Unexpected properties from known building blocks. ACS Macro Lett. 2, 597–600 (2013). · DOI
  32. Seuring, J. & Agarwal, S. Polymers with upper critical solution temperature in aqueous solution. Macromol. Rapid Commun. 33, 1898–1920 (2012). · DOI
  33. Azzaroni, O., Brown, A. A. & Huck, W. T. UCST wetting transitions of polyzwitterionic brushes driven by self-association. Angew. Chem. 118, 1802–1806 (2006). · DOI
  34. Lowe, A. B. & McCormick, C. L. Synthesis and solution properties of zwitterionic polymers. Chem. Rev. 102, 4177–4190 (2002). · DOI
  35. Mason, P., Neilson, G., Dempsey, C., Barnes, A. & Cruickshank, J. The hydration structure of guanidinium and thiocyanate ions: Implications for protein stability in aqueous solution. Proc. Natl Acad. Sci. USA 100, 4557–4561 (2003). · DOI
  36. Mahadevi, A. S. & Sastry, G. N. Cation-π interaction: Its role and relevance in chemistry, biology, and material science. Chem. Rev. 113, 2100–2138 (2013). · DOI
  37. Kao, W. J., Lee, D., Schense, J. C. & Hubbell, J. A. Fibronectin modulates macrophage adhesion and FBGC formation: The role of RGD, PHSRN, and PRRARV domains. J. Biomed. Mater. Res. 55, 79–88 (2001). · DOI
  38. Iwamoto, Y. et al. YIGSR, a synthetic laminin pentapeptide, inhibits experimental metastasis formation. Science 238, 1132–1134 (1987). · DOI
  39. Pierschbacher, M. D. & Ruoslahti, E. Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature 309, 30–33 (1983). · DOI
  40. Lee, B. W. et al. Strongly binding cell-adhesive polypeptides of programmable valencies. Angew. Chem. Int. Ed. 49, 1971–1975 (2010). · DOI
  41. van der Lee, R. et al. Classification of intrinsically disordered regions and proteins. Chem. Rev. 114, 6589–6631 (2014). · DOI
  42. Brassart, B. et al. Conformational dependence of collagenase (matrix metalloproteinase-1) up-regulation by elastin peptides in cultured fibroblasts. J. Biol. Chem. 276, 5222–5227 (2001). · DOI
  43. Dreher, M. R. et al. Temperature triggered self-assembly of polypeptides into multivalent spherical micelles. J. Am. Chem. Soc. 130, 687–694 (2008). · DOI
  44. Callahan, D. J. et al. Triple stimulus-responsive polypeptide nanoparticles that enhance intratumoral spatial distribution. Nano Lett. 12, 2165–2170 (2012). · DOI
  45. Crick, S. L., Ruff, K. M., Garai, K., Frieden, C. & Pappu, R. V. Unmasking the roles of N-and C-terminal flanking sequences from exon 1 of huntingtin as modulators of polyglutamine aggregation. Proc. Natl Acad. Sci. USA 110, 20075–20080 (2013). · DOI
  46. Bates, F. S. et al. Multiblock polymers: Panacea or Pandora’s box? Science 336, 434–440 (2012). · DOI · Paper page
  47. Hassouneh, W., Zhulina, E. B., Chilkoti, A. & Rubinstein, M. Elastin-like polypeptide diblock copolymers self-assemble into weak micelles. Macromolecules 48, 4183–4195 (2015). · DOI
  48. Tong, R., Chiang, H. H. & Kohane, D. S. Photoswitchable nanoparticles for in vivo cancer chemotherapy. Proc. Natl Acad. Sci. USA 110, 19048–19053 (2013). · DOI
  49. Wong, C. et al. Multistage nanoparticle delivery system for deep penetration into tumor tissue. Proc. Natl Acad. Sci. USA 108, 2426–2431 (2011). · DOI
  50. Clark, J. I. Self-assembly of protein aggregates in ageing disorders: The lens and cataract model. Phil. Trans. R. Soc. B 368, 20120104 (2013). · DOI
  51. Smith, F. J. et al. Loss-of-function mutations in the gene encoding filaggrin cause ichthyosis vulgaris. Nature Genet. 38, 337–342 (2006). · DOI
  52. Kyte, J. & Doolittle, R. F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105–132 (1982). · DOI
  53. 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 (2010). · DOI

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Metadata

Authors
Quiroz, F. G., & Chilkoti, A.
Venue
Nature Materials
Published
2015-09-21
Volume
14
Issue
11
Pages
1164-1171
ISSN
  • 1476-1122
  • 1476-4660
Cited by
505
References
4
Language
en

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Quiroz, F. G., & Chilkoti, A. (2015). Sequence heuristics to encode phase behaviour in intrinsically disordered protein polymers. Nature Materials. https://doi.org/10.1038/nmat4418

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