Abstract
Type I Collagen is one of the most abundant proteins of the extracellular matrix of the most organs. During chronological aging or in diseases, type I collagen undergoes biochemical and structural changes which can impact biomechanical and physiological properties of organs. In this study, we have investigated the age-related changes in the molecular organization of type I collagen in rat tails tendon using polarized Raman spectroscopy. Our results show that Amide I, amide III as well as the bands related to proline and hydroxyproline are highly sensitive to polarization and age-related. On the other hand, 1453 and 1270 cm−1 do not show any preferential orientation. Depolarization and anisotropic ratios were used to provide information about the changes in orientation of collagen fibers with aging. The anisotropy degree of Raman bands increase from adult to old collagen, indicating a higher collagen fibers alignment to the fascicle backbone axis in old tendons, and consequently a higher straightness of collagen fibers. These data were correlated to those obtained using polarized second harmonic generation technique. Polarized Raman mapping showed a more homogeneous spatial distribution of collagen fibers alignment to the fascicle axis in old tendon. This confirms a higher straightness of collagen fiber with aging.
Highlights
Polarized Raman spectroscopy (PRS) is a new emerging approach to investigate the organization of type I collagen fibers at the molecular level[15,16,17,18,19,20]
We have investigated the age-related changes in the molecular organization, and orientation of collagen in hydrated Rat tail tendons (RTTs) using PRS and pSHG techniques
We aimed in this study i) to identify the highly anisotropic Raman bands of collagen bonds, ii) to find the polarization directions that bring spectral information related to the structural organization of collagen fibers, and iii) to identify those which could be affected by chronological aging
Summary
Polarized Raman spectroscopy (PRS) is a new emerging approach to investigate the organization of type I collagen fibers at the molecular level[15,16,17,18,19,20]. This technique is able to bring very useful information on the anisotropic response of chemical bonds using different polarization directions for excitation and scattered lights. We aimed in this study i) to identify the highly anisotropic Raman bands of collagen bonds, ii) to find the polarization directions that bring spectral information related to the structural organization of collagen fibers, and iii) to identify those which could be affected by chronological aging
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