Acceleration of fibril formation and thermal stabilization of collagen fibrils in the presence of taxifolin (dihydroquercetin)

Bull Exp Biol Med. 2007 Dec;144(6):791-4. doi: 10.1007/s10517-007-0433-z.

Abstract

We studied the effect of flavonoid taxifolin (dihydriquercetin) on the structure and thermal stability of collagen I fibrils. Taxifolin accelerated fibril formation with reconstruction of periodical cross-striation characteristic of these fibrils. Differential scanning calorimetry showed elevation of melting temperature of collagen fibrils formed in neutral or weakly alkaline media, but not of individual tropocollagen molecules in acid medium. Taxifolin capacity to stimulate fibril formation and promote stabilization of fibrillar forms of collagen can be used in medicine.

MeSH terms

  • Animals
  • Calorimetry, Differential Scanning
  • Collagen Type I / chemistry
  • Collagen Type I / drug effects*
  • Collagen Type I / ultrastructure
  • Drug Stability
  • Hot Temperature
  • Microscopy, Electron
  • Quercetin / analogs & derivatives*
  • Quercetin / pharmacology
  • Rats
  • Thermodynamics

Substances

  • Collagen Type I
  • Quercetin
  • taxifolin