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Updated: Nov 16, 2025

Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides
Published on: January 31, 2014
Effect of Heat Level and Expose Time on Denaturation of Collagen Tissues
İrem Deniz Derman1,2, Esat Can Şenel1,2, Onur Ferhanoğlu1
1Electronics and Communication Engineering, Istanbul Technical University, 34469 Istanbul, Turkey.
Introduction:
The applied heat level and expose time are main issues in certain operations/applications, such as a laser assisted tissue welding, preparation of collagen-based biomaterials (films, implants). Therefore, the precise investigation of these parameters is crucial. The results can serve as a guideline to assess potential effects while maintaining the functionality of the collagen structures.
Methods:
Collagen tissues from rat-tail tendon, calfskin, and bones are soaked in buffer solutions, then examined by microscope at different temperature levels.
Results:
Increase in temperature reduced the microscopically observed collagen crimp contrast for calfskin and rat-tail tendons but not for bone tissues. The contrast level for rat tail tendon decreased down to 80% of its initial value at 37, 157, and 266 s for 70, 65, and 60 °C, respectively. The decrease in the crimp contrast was about only 25% and 2% at 55 and 50 °C after 2 h, respectively. 50% drop in contrast level was occurred for the skin samples at 16, 90, 110 and 1900 s for 70, 65, and 60 °C, respectively. The bone samples, did not show any significant differences in contrast levels.
Conclusion:
The observed denaturation behaviours are in line with Arrhenius Law. This study could be expanded on to other types of tissues at wider temperature ranges to make a guideline for biological/medical processes that radiate heat in order to assess their side effects on collagen and other proteins.
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