Thermal denaturation of UV-irradiated wet rat tail tendon collagen.
The thermal helix-coil transition of UV irradiated collagen in rat tail tendon has been investigated by differential scanning calorimetry. During UVB irradiation the tendons were immersed in water to keep the collagen fibers in a fully hydrated condition at all times. UV irradiation induced changes in collagen which caused both stabilization and destabilization of the triple helix in fibers. The helix-coil transition for non-irradiated collagen occurred near 64 degrees C, for irradiated 1 and 3 h at 66 and 67 degrees C, respectively. After irradiating for longer times (20-66 h) the helix-coil transition peak occurred at much lower temperatures. The peak was very broad and suggested that collagen was reduced by UV to different polypeptides of different molecular weight and different lower thermal stabilities. It was caused by the disruption of a network of hydrogen-bonded water molecules surrounding the collagen macromolecule.
Sionkowska
Alina
A
Faculty of Chemistry, N. Copernicus University, 870100 Torun, Poland. as@chem.uni.torun.pl
D000818:Animals; D003094:Collagen / Q000737:chemistry*; D011489:Protein Denaturation / Q000528:radiation effects; D051381:Rats; D013623:Tail / Q000737:chemistry*; D013710:Tendons / Q000737:chemistry*; D014466:Ultraviolet Rays; D014867:Water / Q000737:chemistry
D014867:Water; D003094:Collagen