Stabilization of collagen using plant polyphenol: role of catechin

Int J Biol Macromol. 2005 Oct 30;37(1-2):47-53. doi: 10.1016/j.ijbiomac.2005.08.005. Epub 2005 Sep 23.

Abstract

Collagen, a unique connective tissue protein finds extensive application as biocompatible biomaterial in wound healing, as drug carriers, cosmetics, etc. A work has been undertaken to study the stabilization of type I collagen using the plant polyphenol catechin. Catechin treated collagen fibres showed a shrinkage temperature around 70 degrees C implying that catechin is able to impart thermal stability to collagen. Catechin treated collagen fibres has been found to be stable even after treatment with high concentration of the secondary structural destabilizer, urea. Circular dichroism studies revealed that there is no major alteration in the structure of collagen on treatment with catechin. The study has demonstrated the involvement of hydrogen bonding and hydrophobic interactions as the major forces involved in the stabilization of collagen by the plant polyphenol, catechin.

MeSH terms

  • Animals
  • Binding Sites
  • Biocompatible Materials / chemistry
  • Catechin / chemistry*
  • Collagen / chemistry*
  • Dose-Response Relationship, Drug
  • Drug Carriers
  • Extracellular Matrix / metabolism
  • Flavonoids / chemistry*
  • Hot Temperature
  • Hydrogen Bonding
  • Male
  • Models, Molecular
  • Molecular Conformation
  • Phenols / chemistry*
  • Plant Proteins / chemistry
  • Polymers / chemistry
  • Polyphenols
  • Protein Binding
  • Protein Conformation
  • Protein Structure, Secondary
  • Rats
  • Rats, Wistar
  • Software
  • Spectroscopy, Fourier Transform Infrared
  • Tannins / chemistry
  • Temperature
  • Tendons / pathology
  • Urea / chemistry
  • Wound Healing

Substances

  • Biocompatible Materials
  • Drug Carriers
  • Flavonoids
  • Phenols
  • Plant Proteins
  • Polymers
  • Polyphenols
  • Tannins
  • Catechin
  • Urea
  • Collagen