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Refolding Behavior of Urea-Induced Denaturation Collagen

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Abstract

Exploration of the denaturation and refolding of natural collagen is important for the application of collagen and its denatured products. In this study, using urea as a denaturant, we prepared a denatured natural collagen product and analyzed its structural changes. The denaturation treatment severely destroyed the triple helix conformation of collagen, but had no significant effect on the primary structure of its a chains or the covalent cross-linking between a chains. Next, we observed the refolding behavior of the denatured collagen by removing urea through dialysis. We found that the denatured collagen products from different sources (grass carp skin, bovine tendon) all showed a reconstruction of the triple helix conformation up to 60–75% of the value of natural collagen during the refolding process. The telopeptide did not significantly promote triple helix reconstruction. In conclusion, the reconstruction of the a chains did not perfectly occur in a “head-to-head, tail-to-tail” manner in refolded collagen, as each a chain was participating in the reconstruction of multiple triple helix domains. The refolded collagen still had weak self-assembly ability and formed a unique network-like structure containing small interlaced and closely combined fibers, which shows favorable cell compatibility and potential applications.

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References

  1. K. Lin, D. Zhang, M. H. Macedo, W. Cui, B. Sarmento, and G. Shen, Adv. Funct. Mater., 29, 1804943 (2019).

    Article  Google Scholar 

  2. A. Sorushanova, L. M. Delgado, Z. Wu, N. Shologu, A. Kshirsagar, R. Raghunath, A. M. Mullen, Y. Bayon, A. Pandit, M. Raghunath, and D. I. Zeugolis, Adv. Mater., 31, 1801651 (2019).

    Article  Google Scholar 

  3. Z. Bazrafshan and G. K. Stylios, Int. J. Biol. Macromol., 129, 693 (2019).

    Article  CAS  Google Scholar 

  4. B. Wei, H. Zhong, L. Wang, Y. Liu, Y. Xu, J. Zhang, C. Xu, L. He, and H. Wang, Int. J. Biol. Macromol., 135, 400 (2019).

    Article  CAS  Google Scholar 

  5. C. Xu, X. Wei, F. Shu, X. Li, W. Wang, P. Li, Y. Li, S. Li, J. Zhang, and H. Wang, Int. J. Biol. Macromol., 153, 232 (2020).

    Article  CAS  Google Scholar 

  6. E. Leikina, M. V. Mertts, N. Kuznetsova, and S. Leikin, Proc. Natl. Acad. Sci., 99, 1314 (2002).

    Article  CAS  Google Scholar 

  7. J. Engel and D. J. Prockop, Annu. Rev. Biophys. Biophys. Chem., 20, 137 (1991).

    Article  CAS  Google Scholar 

  8. Y. Ohyabu, S. Yunoki, H. Hatayama, and Y. Teranishi, Int. J. Biol. Macromol., 62, 296 (2013).

    Article  CAS  Google Scholar 

  9. M. P. Drake and A. Veis, Biochemistry, 3, 135 (1964).

    Article  CAS  Google Scholar 

  10. C. Tkocz and K. Kühn, Eur. J. Biochem., 7, 454 (1969).

    Article  CAS  Google Scholar 

  11. H. Hoermann and H. Schlebusch, Biochemistry, 10, 932 (1971).

    Article  CAS  Google Scholar 

  12. K. Kühn, J. Engel, B. Zimmermann, and W. Grassmann, Arch. Biochem. Biophys., 105, 387 (1964).

    Article  Google Scholar 

  13. K. Kühn and B. K. Zimmermann, Arch. Biochem. Biophys., 109, 534 (1965).

    Article  Google Scholar 

  14. M. D. Maser and R. V. Rice, Biochim. Biophys. Acta, 74, 283 (1963).

    Article  CAS  Google Scholar 

  15. Y. Nomura, M. Yamano, and K. Shirai, Journal of Food Science, 60, 1233 (1995).

    Article  CAS  Google Scholar 

  16. T. V. Burjanadze and M. O. Bezhitadze, Biopolymers, 32, 951 (1992).

    Article  CAS  Google Scholar 

  17. Y. P. Dick and A. Nordwig, Arch. Biochem. Biophys., 117, 466 (1966).

    Article  CAS  Google Scholar 

  18. G. Beier and J. Engel, Biochemistry, 5, 2744 (1966).

    Article  CAS  Google Scholar 

  19. D. R. Cooper, A. E. Russell, and G. J. Hart, Biochem. J., 125, 1069 (1971).

    Article  CAS  Google Scholar 

  20. A. E. Russell and D. R. Cooper, Biochemistry, 8, 3980 (1969).

    Article  CAS  Google Scholar 

  21. A. E. Russell and D. R. Cooper, Biochem. J., 127, 855 (1972).

    Article  CAS  Google Scholar 

  22. A. E. Russell and D. R. Cooper, Biochem. J., 113, 221 (1969).

    Article  CAS  Google Scholar 

  23. J. P. Busnel, E. R. Morris, and S. B. Ross-Murphy, Int. J. Biol. Macromol., 11, 119 (1989).

    Article  CAS  Google Scholar 

  24. J. Engel, Arch. Biochem. Biophys., 97, 150 (1962).

    Article  CAS  Google Scholar 

  25. H. Wang, Y. Liang, H. Wang, H. Zhang, M. Wang, and L. Liu, J. Aquat. Food Prod. Technol., 23, 264 (2014).

    Article  CAS  Google Scholar 

  26. B. Wei, Z. Zhai, H. Wang, J. Zhang, C. Xu, Y. Xu, L. He, and D. Xie, J. Agric. Food Chem., 66, 9080 (2018).

    Article  CAS  Google Scholar 

  27. M. Sun, X. Wei, H. Wang, C. Xu, B. Wei, J. Zhang, L. He, Y. Xu, and S. Li, Food Bioprocess Technol., 13, 367 (2020).

    Article  CAS  Google Scholar 

  28. F. Shu, C. Dai, H. Wang, C. Xu, B. Wie, J. Zhang, Y. Xu, L. He, and S. Li, ChemistrySelect, 4, 13370 (2019).

    Article  CAS  Google Scholar 

  29. Y. Jia, H. Wang, H. Wang, Y. Li, M. Wang, and J. Zhou, Food Sci. Biotechnol., 21, 1585 (2012).

    Article  CAS  Google Scholar 

  30. B. Wei, J. Nan, Y. Jiang, H. Wang, J. Zhang, L. He, C. Xu, Z. Zhai, D. Xie, and S. Xie, Food Biophys., 12, 422 (2017).

    Article  Google Scholar 

  31. J. Zhang, M. Zou, M. Zhang, B. Wei, C. Xu, D. Xie, and H. Wang, Food Biophys., 11, 380 (2016).

    Article  Google Scholar 

  32. L. Niu, S. E. Jee, K. Jiao, L. Tonggu, M. Li, L. Wang, Y.-D. Yang, J.-H. Bian, L. Breschi, S. S. Jang, J.-H. Chen, D. H. Pashley, and F. R. Tay, Nat. Mater., 16, 370 (2017).

    Article  CAS  Google Scholar 

  33. H. Yang, H. Wang, Y. Zhao, H. Wang, and H. Zhang, J. Sci. Food Agric., 95, 329 (2015).

    Article  CAS  Google Scholar 

  34. J. Bella, Biochem. J., 473, 1001 (2016).

    Article  CAS  Google Scholar 

  35. B. De C. Vidal, M. L. S. Mello, and É. R. Pimentel, Histochem. J., 14, 857 (1982).

    Article  CAS  Google Scholar 

  36. V. S. Constantine and R. W. Mowry, J. Invest. Dermatol., 50, 419 (1968).

    Article  CAS  Google Scholar 

  37. K. E. Kadler, Y. Hojima, and D. J. Prockop, J. Biol. Chem., 263, 10517 (1988).

    Article  CAS  Google Scholar 

  38. S. Leikin, D. C. Rau, and V. A. Parsegian, Nat. Struct. Biol., 2, 205 (1995).

    Article  CAS  Google Scholar 

  39. K. Kar, P. Amin, M. A. Bryan, A. V. Persikov, A. Mohs, Y.-H. Wang, and B. Brodsky, J. Biol. Chem., 281, 33283 (2006).

    Article  CAS  Google Scholar 

Download references

Acknowledgments

This research was supported by the National Natural Science Foundation of China (Nos. 21676208, 21706201), the Natural Science Foundation of Hubei Province (Nos. 2018CFA030, 2019CFB252), and the Application Foundation Frontier Project of Wuhan Science and Technology Bureau (No. 2019020701011478).

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Correspondence to Chengzhi Xu or Haibo Wang.

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Information is available regarding TGA and DTG curves of collagen samples, the CD temperature scanning curves and their derivative curves of collagen samples. The materials are available via the Internet at http://www.springer.com/13233.

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Wei, X., Zhao, Y., Zheng, J. et al. Refolding Behavior of Urea-Induced Denaturation Collagen. Macromol. Res. 29, 402–410 (2021). https://doi.org/10.1007/s13233-021-9047-y

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