Dielectric properties of the collagen-glycosaminoglycans scaffolds in the temperature range of thermal decomposition

Biophys Chem. 2005 Oct 22;118(1):51-6. doi: 10.1016/j.bpc.2005.07.006.

Abstract

Dielectric spectroscopy has been applied to study the decomposition process of unmodified collagen and chondroitin sulfate (CS)- and hyaluronic acid (HA)-modified collagen. Measurements were performed over the frequency range from 10 Hz to 100 kHz and at temperatures from 22 to 260 degrees C. According to the Kramers-Kronig relationship a dispersion is apparent in both epsilon' and epsilon'' for the three materials below 140 degrees C and at higher temperatures as a broad peak around 220-230 degrees C, respectively. The values of epsilon' and epsilon'' at the same temperature for constant frequency are higher in HA-modified collagen than in the unmodified collagen. However, small differences are shown in these parameters between CS-modified collagen and unmodified collagen. The observed dispersion around 220-230 degrees C corresponds to the decomposition of unmodified and CS- and HA-modified collagen. Power-low responses are observed for the frequency dependence of ac conductivity for unmodified and modified collagen. The behaviour observed for temperature dependencies of the exponent n for the three materials is considered to be related to the proton polarization and conduction processes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Collagen / chemistry*
  • Electric Conductivity*
  • Glycosaminoglycans / chemistry*
  • Protons
  • Spectrum Analysis / methods
  • Thermodynamics
  • Time Factors

Substances

  • Glycosaminoglycans
  • Protons
  • Collagen