Stability of collagen gel after uv irradiation

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Resumo

Type I collagen is the most abundant extracellular matrix protein in the human body, as well as is the main structural element in tissues and regulates cellular functions. In lifetime, the organism and extracellular matrix components such as collagen are exposed to UV irradiation. The purpose of this work was to study the effect of UV irradiation on the stability and structure of collagen fibrils. It has been shown that UV irradiation has a stabilization effect on collagen gel at a concentration of 0.5 mg/ml. Scanning electron microscope images have shown that the diameter of the collagen fibrils is not changed after UV irradiation. The degree of spreading of cells cultured on collagen fibrils after UV irradiation is greater compared to those cultured on collagen fibrils unirradiated with UV light. UV irradiation promotes a shift of the collagen amide A band to lower frequency, indicating that it induces structural changes in collagen.

Sobre autores

Yu. Nashchekina

Institute of Cytology, Russian Academy of Sciences;Ioffe Institute, Russian Academy of Sciences

Email: nashchekina.yu@mail.ru
St. Petersburg, Russia

N. Trusova

Institute of Cytology, Russian Academy of Sciences

St. Petersburg, Russia

P. Nikonov

Institute of Cytology, Russian Academy of Sciences

St. Petersburg, Russia

A. Nashchekin

Ioffe Institute, Russian Academy of Sciences

N. Mikhailova

Institute of Cytology, Russian Academy of Sciences

St. Petersburg, Russia

Bibliografia

  1. A. Bailey and R. Paul, J. Soc. Leather Technol. Chem., 82, 104 (1998).
  2. S. Ricard, Perspect. Biol., 1, 3 (2011).
  3. S. Ricard-Blum, Perspect. Biol., 3, 1 (2011).
  4. Yu. А. Nashchekina, А. А. Starostina, N. А. Trusova, et al., J. Physics: Conf. Series, 1697, 012053 (2020).
  5. A. Amaro-Ortiz, B. Yan, and J. A. D'Orazio, Molecules, 19, 6202 (2014).
  6. Yu. A. Nashchekina, N. M. Yudintceva, P. O. Nikonov, et al., Bull. Exp. Biol. Med., 163, 123 (2017).
  7. M. G. Haugh, C. M. Murphy, R. C. McKiernan, et al., Tissue. Eng. Part A, 17, 1201 (2011).
  8. Y. Hu, L. Liu, W. Dan, et al., Int. J. Biol. Macromol., 55, 221 (2013).
  9. S. J. Hollister and R. D. T. Maddox, J. Biomater., 23, 4095 (2002).
  10. J. S. Pieper, T. Hafmans, J. H. Veerkamp, et al. Biomaterials, 21, 581 (2000).
  11. M. G. Haugh., PhD Thesis (Trinity Colledge, Dublin University, Ireland, 2008).
  12. D.-H. Lew, P. H-T. Liu, and D. P. Orgill, J. Biomed. Mater. Res. B. Appl. Biomater., 82, 51 (2007).
  13. L. H. Olde Damink, P. J. Dijkstra, M. J. van Luyn, et al., Biomaterials, 17, 765 (1996).
  14. N. Davidenko, D. V. Bax, C. F. Schuster, et al., Mater. Sci.: Mater. Med., 27,14 (2016).
  15. N. Metreveli, L. Namicheishvili, K. Jariashvili, et al., Int. J. Photoenergy, 76830, 1 (2006).
  16. M. P. Ohan, K. S. Weadock, and M. G. Dunn, J. Biomed. Mater. Res., 60, 384 (2002).
  17. G. Chandrakasan, D. A. Torchia, K. A. Piez, J. Biol. Chem., 251, 6062 (1976).
  18. O. H. Lowry, N. J. Rosbrough, A. L. Farr, and R. J. Randall, J. Biol. Chem., 193, 265. (1951).
  19. Y. Nashchekina, A. Chabina, A. Nashchekin, et al., Polymers, 12, 1042 (2020).
  20. A. Sionkowska, J. Photoch. Photobiol. B: Biology, 82, 9 (2006).
  21. A. Kaminska and A. Sionkowska, Pol. Degr. Stability, 51,19 (1996).

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