Acceleration of fibril formation and thermal stabilization of collagen fibrils in the presence of taxifolin (dihydroquercetin).
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.
Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino. tarahov@rambler.ru
Y S
YS
Tarahovsky
I I
II
Selezneva
N A
NA
Vasilieva
M A
MA
Egorochkin
Yu A
YA
Kim
D000818:Animals; D002152:Calorimetry, Differential Scanning; D024042:Collagen Type I / Q000737:chemistry / Q000187:drug effects* / Q000648:ultrastructure; D004355:Drug Stability; D006358:Hot Temperature; D008854:Microscopy, Electron; D011794:Quercetin / Q000031:analogs & derivatives* / Q000494:pharmacology; D051381:Rats; D013816:Thermodynamics
D024042:Collagen Type I; D011794:Quercetin; C003377:taxifolin