Spectroscopic investigation of the skin deformation influence on the shiff base content in the 1st collagen type that is synthesizing

  • Т. V. Kostina Department of Biochemsitry, V.N. Karazin Kharkiv National University
  • J. G. Kot Department of Biochemsitry, V.N. Karazin Kharkiv National University
  • М. V. Goenaga Department of Biochemsitry, V.N. Karazin Kharkiv National University
  • N. А. Nikitina Department of Biochemsitry, V.N. Karazin Kharkiv National University
  • Е. A. Persky Department of Biochemsitry, V.N. Karazin Kharkiv National University
Keywords: 1st type of collagen, synthesis, Schiff bases, fluorimetry, IR-spectroscopy

Abstract

The influence of connective tissue cell deformation in the skin of 3-month old rats vas investigated in vitro
after its mechanical stretch of (0,075 – 0,18) MH/m2. Experiments were performed with. fluorimetry and
IR-spectroscopy. The Schiff bases content was determined in the 1st collagen type, which was synthesized at
stretch conditions. For determining all Schiff base molecules which can be created in the collagen
supramolecular structures, the semicarbazide was added into the incubation medium. Semicarbazide amino groups were condensed with the aldehyde groups of al-lysine and hydroxyl-al-lysine resulting in the Schiff bases formation already in the new collagen molecules that were deprived of molecular aggregates.
Fluorescent spectra of de novo synthesized 1st collagen type have been demonstrated the decreased emission intensity at λ =430 nm (Schiff bases characteristic wavelength) at the increasing of stretch in the skin. The intensity of 1st type collagen absorption band at 1640 cm-1 in the IR spectra was analyzed. It is the
characteristic frequency of Schiff bases in the collagen triple helix. This band absorption intensity in the
collagen was decreased with the increase of stress when collagen was synthesized in the skin. Schiff base
content of the collagen structures is inverse to the mechanical stress in the tissue. At stress grows from 0 to 0,15 MN/m2 Schiff base content diminishes to 39,2% and 33,0% respectively according to fluorescent and IR spectroscopic data.

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Author Biographies

Т. V. Kostina, Department of Biochemsitry, V.N. Karazin Kharkiv National University

4 Svobody square, Kharkiv 61077, Ukraine
epersky@list.ru

J. G. Kot, Department of Biochemsitry, V.N. Karazin Kharkiv National University

4 Svobody square, Kharkiv 61077, Ukraine
epersky@list.ru

М. V. Goenaga, Department of Biochemsitry, V.N. Karazin Kharkiv National University

4 Svobody square, Kharkiv 61077, Ukraine
epersky@list.ru

N. А. Nikitina, Department of Biochemsitry, V.N. Karazin Kharkiv National University

4 Svobody square, Kharkiv 61077, Ukraine
epersky@list.ru

Е. A. Persky, Department of Biochemsitry, V.N. Karazin Kharkiv National University

4 Svobody square, Kharkiv 61077, Ukraine
epersky@list.ru

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Published
2009-06-05
Cited
How to Cite
KostinaТ. V., Kot, J. G., GoenagaМ. V., NikitinaN. А., & PerskyЕ. A. (2009). Spectroscopic investigation of the skin deformation influence on the shiff base content in the 1st collagen type that is synthesizing. Biophysical Bulletin, 2(23), 46-51. Retrieved from https://periodicals.karazin.ua/biophysvisnyk/article/view/4363