Collagen type I amide I band infrared spectroscopy

Micron. 2011 Apr;42(3):283-9. doi: 10.1016/j.micron.2010.09.010. Epub 2010 Nov 18.

Abstract

Collagen fiber structure and organization have been found to vary in different tendon types. Differences have been reported in the FT-IR spectra of the amide I band of collagen-containing structures. In the present study, the FT-IR spectral characteristics of the amide I band of the bovine flexor tendon and the extended rat tail tendon were compared by using the diamond attenuated total reflectance technique. The objective was to associate FT-IR spectral characteristics in tendons with their different collagen fiber supraorganization and biomechanical properties. Nylon 6 and poly-L-lysine were used as polyamide models. Each of these materials was found to exhibit molecular order and crystallinity, as revealed by their birefringence. The following FT-IR parameters were evaluated: amide I band profile, absorption peaks and areas, and the 1655 cm⁻¹/1690 cm⁻¹ absorbance ratio. The amide I area and the 1655 cm⁻¹/1690 cm⁻¹ absorbance ratio were significantly higher for the bovine flexor tendon, indicating that its collagen fibers are richer in pyridinoline-type cross-linking, proline and/or hydroxyproline and H-bonding, and that these fibers are more packed and supraorganizationally ordered than those in the rat tail tendon. This conclusion is additionally supported by differences in collagen solubility and biochemical/biomechanical properties of the tendons.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amides / chemistry*
  • Animals
  • Anisotropy
  • Cattle
  • Collagen Type I / chemistry*
  • Microscopy, Polarization
  • Rats
  • Spectroscopy, Fourier Transform Infrared*

Substances

  • Amides
  • Collagen Type I