Thermal (in)stability of type I collagen fibrils

• Published in: Physical review letters Vol. 102; no. 4; p. 048101
• Main Authors: Gevorkian, S G, Allahverdyan, A E, Gevorgyan, D S, Simonian, A L
• Format: Journal Article
• Language: English
• Published: United States 30-01-2009
• Subjects: Achilles Tendon - chemistry; Achilles Tendon - ultrastructure; Animals; Collagen Type I - chemistry; Collagen Type I - isolation & purification; Drug Stability; Elasticity; Protein Conformation; Rats; Temperature; Viscosity
• ISSN: 0031-9007; 1079-7114
• DOI: 10.1103/physrevlett.102.048101

We measured the Young's modulus at temperatures ranging from 20 to 100 degrees C for a collagen fibril that is taken from a rat's tendon. The hydration change under heating and the damping decrement were measured as well. At physiological temperatures 25 to 45 degrees C, the Young's modulus decreases, which can be interpreted as an instability of the collagen. For temperatures between 45 and 80 degrees C, the Young's modulus first stabilizes and then increases when the temperature is increased. The hydrated water content and the damping decrement have strong maximums in the interval 70 to 80 degrees C indicating complex intermolecular structural changes in the fibril. All these effects disappear after heat-denaturation of the sample at 120 degrees C. Our main achievement is a five-stage mechanism by which the instability of a single collagen at physiological temperatures is compensated by the interaction between collagen molecules.