Skip to main content
SpringerLink
Log in

Heat-induced coacervation of elastin and its possible thermoreversibility

  • Original Contribution
  • Published:
Colloid and Polymer Science Aims and scope Submit manuscript

Abstract

Elastin (E) coacervation was studied close to isoelectric pH (pI = 4.7 ± 0.5), and this thermally activated self-assembly leading to phase separation involved the following three distinguishable temperatures: onset of interpolymer interaction at Tos, coacervation at Tc, and mesophase separation at Tms. Such behavior was absent in elastin solutions made at other pHs. The pH-dependent particle size histogram revealed bimodal distribution between pH 2 to 4 and 5.5 to 6.2, whereas the region pH = pI ± 0.5, a coacervate-rich domain with trimodal size distribution. The coacervation temperature TC decreased from 38 to 33 °C with increase in solution ionic strength (0–40 mM, NaCl) implying the importance of hydrophobic forces that governed the molecular self-assembly. The thermoreversibility of the turbidity profile implied that the elastin complexes did not fully dissociate into their monomeric state upon temperature reversal. Two observations were made here: (i) the hysteresis loop formed by the heating-cooling cycle had an area that decreased with ionic strength of the solution and (ii) the remnant aggregated E content increased with solution ionic strength. The present study highlights some of the key issues related to the reversibility of self-assembled soft matter systems which remains somewhat poorly explored until now.

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

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5
Fig. 6
Fig. 7
Fig. 8
Fig. 9
Fig. 10
Fig. 11
Scheme 1

Similar content being viewed by others

References

  1. De Jong HB, Kruyt HR (eds) (1949) Colloid science, 2. Elsevier, London, pp 232–238

    Google Scholar 

  2. De Jong HB, Bonner J (1935) Phosphatide auto-complex coacervates as ionic systems and their relation to the protoplasmic membrane. Protoplasma 24(1):198–218

    Article  Google Scholar 

  3. Dubin P, Stewart RJ (2018) Complex coacervation. Soft Matter 14:329–330

    Article  CAS  PubMed  Google Scholar 

  4. Lytle TK, Sing CE (2018) Tuning chain interaction entropy in complex coacervation using polymer stiffness, architecture, and salt valency. Mol Syst Des Eng 3:183–196

    Article  CAS  Google Scholar 

  5. Rawat K, Bohidar HB (2014) Coacervation in biopolymers. J Phys Chem Biophys 4(6):1

    Google Scholar 

  6. Cooper CL, Dubin PL, Kayitmazer AB, Turksen S (2005) Polyelectrolyte–protein complexes. Curr Opin Colloid Interface Sci 10:52–78

    Article  CAS  Google Scholar 

  7. Pathak J, Priyadarshini E, Rawat K, Bohidar HB (2017) Complex coacervation in charge complementary biopolymers: electrostatic versus surface patch binding. Adv Colloid Interf Sci 250:40–53

    Article  CAS  Google Scholar 

  8. Elhassan MS, Oguntoyinbo SI, Taylor J, Taylor JR (2018) Formation and properties of viscoelastic masses made from kafirin by a process of simple coacervation from solution in glacial acetic acid using water. Food Chem 239:333–342

    Article  CAS  PubMed  Google Scholar 

  9. Danielsen S, Delaney K, Fredrickson G (2018) Small ion effects on self-coacervation phenomena in block polyampholytes. Bull Am Phys Soc

  10. Rodriguez AMB, Binks BP, Sekine T (2018) Emulsion stabilisation by complexes of oppositely charged synthetic polyelectrolytes. Soft Matter 14(2):239–254

    Article  Google Scholar 

  11. Li Y, Dubin PL, Havel HA, Edwards SL, Dautzenberg H (1995) Complex formation between polyelectrolyte and oppositely charged mixed micelles: soluble complexes vs coacervation. Langmuir 11(7):2486–2492

    Article  CAS  Google Scholar 

  12. Kizilay E, Kayitmazer AB, Dubin PL (2011) Complexation and coacervation of polyelectrolytes with oppositely charged colloids. Adv Colloid Interf Sci 167(1–2):24–37

    Article  CAS  Google Scholar 

  13. Imeson AP, Watson APR, Mitchell JR, Ledward DA (1978) Protein recovery from blood plasma by precipitation with polyuronates. Int J Food Sci Technol 13(4):329–338

    Article  CAS  Google Scholar 

  14. Tolstoguzov VB (1991) Functional properties of food proteins and role of protein-polysaccharide interaction. Food Hydrocoll 4(6):429–468

    Article  CAS  Google Scholar 

  15. De Kruif CG, Weinbreck F, de Vries R (2004) Complex coacervation of proteins and anionic polysaccharides. Curr Opin Colloid Interface Sci 9(5):340–349

    Article  CAS  Google Scholar 

  16. Xiao Z, Liu W, Zhu G, Zhou R, Niu Y (2014) A review of the preparation and application of flavour and essential oils microcapsules based on complex coacervation technology. J Sci Food Agric 94(8):1482–1494

    Article  CAS  PubMed  Google Scholar 

  17. Dai R, Wu G, Li W, Zhou Q, Li X, Chen H (2010) Gelatin/carboxymethylcellulose/dioctyl sulfosuccinate sodium microcapsule by complex coacervation and its application for electrophoretic display. Colloids Surf A Physicochem Eng Asp 362(1–3):84–89

    Article  CAS  Google Scholar 

  18. Moschakis T, Biliaderis CG (2017) Biopolymer-based coacervates: structures, functionality and applications in food products. Curr Opin Colloid Interface Sci 28:96–109

    Article  CAS  Google Scholar 

  19. Tiwari A, Bindal S, Bohidari HB (2008) Kinetics of protein-protein complex coacervation and biphasic release of salbutamol sulfate from coacervate matrix. Biomacromolecules 10(1):184–189

    Article  CAS  Google Scholar 

  20. Mohanty B, Bohidar HB (2003) Systematic of alcohol-induced simple coacervation in aqueous gelatin solutions. Biomacromolecules 4(4):1080–1086

    Article  CAS  PubMed  Google Scholar 

  21. Gupta A, Bohidar HB (2005) Kinetics of phase separation in systems exhibiting simple coacervation. Phys Rev E 72(1):011507

    Article  CAS  Google Scholar 

  22. Kaibara K, Okazaki T, Bohidar HB, Dubin PL (2000) pH-induced coacervation in complexes of bovine serum albumin and cationic polyelectrolytes. Biomacromolecules 1(1):100–107

    Article  CAS  PubMed  Google Scholar 

  23. Maeda T, Takenouchi M, Yamamoto K, Aoyagi T (2006) Analysis of the formation mechanism for thermoresponsive-type coacervate with functional copolymers consisting of N-isopropylacrylamide and 2-hydroxyisopropylacrylamide. Biomacromolecules 7:2230–2236

    Article  CAS  PubMed  Google Scholar 

  24. Wolf T, Rheinberger T, Wurm FR (2017) Thermoresponsive coacervate formation of random poly (phosphonate) terpolymers. Eur Polym J 95:756–765

    Article  CAS  Google Scholar 

  25. Swanson JP, Monteleone LR, Haso F, Costanzo PJ, Liu T, Joy A (2015) A library of thermoresponsive, coacervate-forming biodegradable polyesters. Macromolecules 48:3834–3842

    Article  CAS  Google Scholar 

  26. Maeda I, Fukumoto Y, Nose T, Shimohigashi Y, Nezu T, Terada Y, Kodama H, Kaibara K, Okamoto K (2011) Structural requirements essential for elastin coacervation: favorable spatial arrangements of valine ridges on the three-dimensional structure of elastin-derived polypeptide (VPGVG) n. J Pept Sci 17(11):735–743

    Article  CAS  PubMed  Google Scholar 

  27. Betre H, Setton LA, Meyer DE, Chilkoti A (2002) Characterization of a genetically engineered elastin-like polypeptide for cartilaginous tissue repair. Biomacromolecules 3:910–916

    Article  CAS  PubMed  Google Scholar 

  28. Meyer DE, Shin BC, Kong GA, Dewhirst MW, Chilkoti A (2001) Drug targeting using thermally responsive polymers and local hyperthermia. J Control Release 74:213–224

    Article  CAS  PubMed  Google Scholar 

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

    Article  CAS  Google Scholar 

  30. Herrero-Vanrell R, Rincon AC, Alonso M, Reboto V, Molina-Martinez IT, Rodriguez-Cabello JC (2005) Self-assembled particles of an elastin-like polymer as vehicles for controlled drug release. J Control Release 102:113–122

    Article  CAS  PubMed  Google Scholar 

  31. Yeo GC, Keeley FW, Weiss AS (2011) Coacervation of tropoelastin. Adv Colloid Interf Sci 167(1–2):94–103

    Article  CAS  Google Scholar 

  32. Bohidar HB (2002) Characterization of polyelectrolytes by dynamic light scattering Handbook of Polyelectrolytes, vol II. American Scientific Publishers, California

    Google Scholar 

  33. Baldock C, Oberhauser AF, Ma L, Lammie D, Siegler V, Mithieux SM, Tu Y, Chow JYH, Suleman F, Malfois M, Rogers S (2011) Shape of tropoelastin, the highly extensible protein that controls human tissue elasticity. Proc Natl Acad Sci 108(11):4322–4327

    Article  PubMed  Google Scholar 

  34. Graham JS, Vomund AN, Phillips CL, Grandbois M (2004) Structural changes in human type I collagen fibrils investigated by force spectroscopy. Exp Cell Res 299(2):335–342

    Article  CAS  PubMed  Google Scholar 

  35. Clarke AW, Arnspang EC, Mithieux SM, Korkmaz E, Braet F, Weiss AS (2006) Tropoelastin massively associates during coacervation to form quantized protein spheres. Biochemistry 45(33):9989–9996

    Article  CAS  PubMed  Google Scholar 

  36. Bellingham CM, Woodhouse KA, Robson P, Rothstein SJ, Keeley FW (2001) Self-aggregation characteristics of recombinantly expressed human elastin polypeptides. Biochim Biophys Acta (BBA) Protein Struct Mol Enzymol 1550(1):6–19

    Article  CAS  Google Scholar 

  37. Jamieson AM, Downs CE, Walton AG (1973) Studies of elastin coacervation by quasi-elastic light scattering. Biochim Biophys Acta 271:34–47

    Article  Google Scholar 

  38. Kjaergaard M, Nørholm AB, Hendus–Altenburger R, Pedersen SF, Poulsen FM, Kragelund BB (2010) Temperature-dependent structural changes in intrinsically disordered proteins: formation of α–helices or loss of polyproline II? Protein Sci 19(8):1555–1564

    Article  CAS  PubMed  PubMed Central  Google Scholar 

Download references

Acknowledgments

PK is thankful to the University Grant Commission, Government of India UGC, for a Senior Research Fellowship. KR is thankful to the Department of Science and Technology, Government of India, for the DST-Inspire Faculty Award. We are thankful to the Advanced Instrumentation Research facility (AIRF) for allowing to access their instrument.

Funding

This study was funded by the Department of Science and Technology (DST), Government of India under the DST-PURSE-II Program.

Author information

Authors and Affiliations

  1. School of Physical Sciences, Jawaharlal Nehru University, New Delhi, India

    Priyanka Kaushik & H. B. Bohidar

  2. Department of Chemistry, School of Chemical and Life Sciences, Jamia Hamdard, New Delhi, India

    Kamla Rawat

Authors
  1. Priyanka Kaushik
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Kamla Rawat
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. H. B. Bohidar
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding authors

Correspondence to Kamla Rawat or H. B. Bohidar.

Ethics declarations

Conflict of interest

The authors declare that they no conflict of interest.

Additional information

Publisher’s note

Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Kaushik, P., Rawat, K. & Bohidar, H.B. Heat-induced coacervation of elastin and its possible thermoreversibility. Colloid Polym Sci 297, 947–956 (2019). https://doi.org/10.1007/s00396-019-04518-1

Download citation

  • Received:

  • Revised:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s00396-019-04518-1

Keywords

Search

Navigation