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Mechanobiology of soft tissues: FT-Raman spectroscopic studies

Treść / Zawartość
Identyfikatory
Warianty tytułu
Języki publikacji
EN
Abstrakty
EN
FT-Raman spectroscopy was used to investigate microstructural changes in the secondary protein structure of soft tissues subjected to increasing levels of macroscopic strain. Main protein bands at 938 cm-1 assigned as v(Cα–C), 1668 cm-1 — amide I and 1268 cm-1 — amide III are sensitive to applied strain and undergo wavenumber shifting. Other main vibrational modes at 1004 cm-1 assigned to the phenyl ring breathing mode and 2940 cm-1 (n(CH3,CH2)) remain unaltered. Spectroscopic results were compared with the mechanical relations obtained from the standard protocol of uniaxial tensile tests carried out in a testing machine. A clear correlation between Raman band shifting and the level of mechanical stress was established. Initially the load is transferred through elastin and then gradually also by collagen. It was proved that transferring loads by soft tissues involves changes in structural protein conformation. This process was described in detail for a tendon. It was also confirmed that mechanical properties of soft tissues depend on collagen and elastin fiers orientation.
Rocznik
Strony
8--11
Opis fizyczny
Bibliogr. 13 poz., wykr.
Twórcy
  • Institute of Biomedical Engineering and Instrumentation, Faculty of Fundamental Problems of Technology, Wrocław University of Technology, Wrocław, Poland
  • Regional Specialist Hospital in Wroclaw, Research and Development Center, ul. Kamieńskiego 73a, 51-124 Wrocław, Poland
  • Institute of Biomedical Engineering and Instrumentation, Faculty of Fundamental Problems of Technology, Wrocław University of Technology, Wrocław, Poland
autor
  • Department of Bioorganic Chemistry, Wrocław University of Economics, Wrocław, Poland
autor
  • Institute of Low Temperature and Structure Research, Polish Academy of Sciences, 50-950 Wrocław 2, Poland
  • Division of Biomedical Engineering and Experimental Mechanics, Institute of Machine Design and Operation, Faculty of Mechanical Engineering, Wrocław University of Technology, Wrocław, Poland
  • Regional Specialist Hospital in Wroclaw, Research and Development Center, ul. Kamieńskiego 73a, 51-124 Wrocław, Poland
autor
  • Division of Biomedical Engineering and Experimental Mechanics, Institute of Machine Design and Operation, Faculty of Mechanical Engineering, Wrocław University of Technology, Wrocław, Poland
  • Regional Specialist Hospital in Wroclaw, Research and Development Center, ul. Kamieńskiego 73a, 51-124 Wrocław, Poland
Bibliografia
  • [1] Beana, J.R., and B. Lendl. “Raman spectroscopy in chemical bioanalysis.” Current Opinion in Chemical Biology 8 (2004): 534–539.
  • [2] Church, J.S., G.L. Corino, and A.L. Woodhead. “The effects of stretching on wool fi bres as monitored by FTRaman spectroscopy.” Journal of Molecular Structure 440 (1998): 15–23.
  • [3] Debelle, L., et al. “The secondary structure and architecture of human elastin.” European Journal of Biochemistry 258 (1998): 533–539.
  • [4] Dong, R., et al. “Temperature-dependent Raman spectra of collagen and DNA.” Spectrochimica Acta Part A 60 (2004): 557–561.
  • [5] Hanuza, J., et al. “FT-Raman spectroscopic study of thoracic aortic wall subjected to uniaxial stress.” Journal of Raman Spectroscopy 40 (2009).
  • [6] Manoharan, R., Y. Wang, and M.S. Feld. “Histochemical analysis of biological tissues using Raman spectroscopy.” Spectrochimica Acta A 52 (1996): 215–249.
  • [7] Pappas, D., B.W. Smith, and J.D. Winefordner. “Raman spectroscopy in bioanalysis.” Talanta 51 (2000): 131–144.
  • [8] Silver, F.H., J.W. Freeman, and G.P. Seehra. “Collagen sel-assembly and the development of tendon mechanical properties”. Journal of Biomechanics 36 (2003): 1529–1553.
  • [9] Sirichaisit, J., R.J. Young, and F. Vollrath. “Molecular deformation in spider dragline silk subjected to stress.” Polymer 41 (2000): 1223–1227.
  • [10] van Zuijlen, P.P.M., et al. “Collagen morphology in human skin and scar tissue: no adaptations in response to mechanical loading at joints.” Burns 29 (2003): 423–431.
  • [11] Vouyouka, A.G., et al. “The role of type I collagen in aortic wall strength with a homotrimeric [α1(I)]3 collagen mouse model”. Journal of Vascular Surgery 33 (2001): 1263–1270.
  • [12] Wang, J.H.-C. “Mechanobiology of tendon.” Journal of Biomechanics 39 (2006): 1563–1582.
  • [13] Wang, Y.-N., C. Galiotis, and D.L. Bader. “Determination of molecular changes in soft tissues under strain using laser Raman microscopy”. Journal of Biomechanics 33 (2000), 483–486.
Typ dokumentu
Bibliografia
Identyfikator YADDA
bwmeta1.element.baztech-0c304bfb-a63c-4f08-bf72-982c937afd0e
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