Interaction of collagen with corilagin

The molecular mechanism of the stabilization of collagen with hydrolyzable tannin, corilagin, has been investigated using techniques like centrifugation, shrinkage temperature, infrared spectroscopy, and differential scanning calorimetry. Thermodynamic measurements were also carried out for the collagen-corilagin interaction. Results of this study indicate the enthalpic nature of non-specific binding of collagen with corilagin. The shrinkage temperature increases linearly with corilagin, indicating that the helix-to-coil transition is hindered by corilagin interaction with collagen triple helix. This study suggests that ingested polyphenols (corilagin) alter the stability of the proline-rich protein in the gut. Thereby, the stability of collagen present in the serosa layer may be hindered.