Collagen type I amide I band infrared spectroscopy

• Grant number: 11/00329-7
• Support Opportunities: Regular Research Grants - Publications - Scientific article
• Start date: March 01, 2011
• End date: August 31, 2011
• Field of knowledge: Biological Sciences - Morphology - Cytology and Cell Biology
• Principal Investigator: Benedicto de Campos Vidal
• Grantee: Benedicto de Campos Vidal
• Host Institution: Instituto de Biologia (IB). Universidade Estadual de Campinas (UNICAMP). Campinas , SP, Brazil
• City of the host institution: Campinas

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 theextended 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 theirbirefringence. The following FT-IR parameters were evaluated: amide I band profile, absorption peaks and areas, and the 1655cm1/1690cm1 absorbance ratio. The amide I area and the 1655cm1/1690cm1 absorbance ratio were significantly higher for the bovine flexor tendon, indicating that its collagen fibersare 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. (AU)