[Formation of collagen type I fibrils in vitro].
The assembly of collagen fibrils as a function of temperature and collagen concentration was studied. It was shown that temperature increases from 25 to 35 degrees C, the degree of ordering of collagen fibrils increases 1.5-fold at collagen concentration above 1 mg/ml and 2-fold at low collagen concentration. A maximum ordering of fibril structure occurs under conditions close to physiological (T approximately 35 degrees C and collagen concentration 1.2 mg/ml). As temperature is elevated from 30 to 35 degrees C, the packing of collagen molecules in fibrils becomes more ordered: the values of enthalpy and entropy of the transition of fibrils from the native to a disordered state decrease at all collagen concentrations used. At high collagen concentration, the dimensions of cooperative blocks in fibrils formed at 25 and 30 degrees C coincide with those of cooperative blocks of monomeric collagen in solution. Upon increasing the temperature to 35 degrees C, the dimensions of cooperative blocks increase.
Nikolaeva
T I
TI
Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Moscow Region, 142290 Russia.
Pisachenko
A I
AI
Polozov
R V
RV
Rochev
Iu A
IuA
Gavriliuk
B K
BK
D000818:Animals; D002152:Calorimetry, Differential Scanning; D003094:Collagen / Q000737:chemistry* / Q000648:ultrastructure; D007700:Kinetics; D051381:Rats; D013053:Spectrophotometry / Q000379:methods; D013696:Temperature; D013816:Thermodynamics
D003094:Collagen