Monitoring the thermally induced structural transitions of collagen by use of second-harmonic generation microscopy.
The thermal disruption of collagen I in rat tail tendon is investigated with second-harmonic generation (SHG) microscopy. We investigate its effects on SHG images and intensity in the temperature range 25 degrees-60 degrees C. We find that the SHG signal decreases rapidly starting at 45 degrees C. However, SHG imaging reveals that breakage of collagen fibers is not evident until 57 degrees C and worsens with increasing temperature. At 57 degrees C, structures of both molten and fibrous collagen exist, and the disruption of collagen appears to be complete at 60 degrees C. Our results suggest that, in addition to intensity measurement, SHG imaging is necessary for monitoring details of thermally induced changes in collagen structures in biomedical applications.
Lin
Sung-Jan
SJ
Institute of Biomedical Engineering, College of Medicine, National Taiwan University, Taipei 100, Taiwan.
Hsiao
Chih-Yuan
CY
Sun
Yen
Y
Lo
Wen
W
Lin
Wei-Chou
WC
Jan
Gwo-Jen
GJ
Jee
Shiou-Hwa
SH
Dong
Chen-Yuan
CY
D000818:Animals; D003094:Collagen / Q000502:physiology* / Q000648:ultrastructure*; D018613:Microscopy, Confocal / Q000379:methods*; D008859:Microscopy, Polarization / Q000379:methods*; D044367:Phase Transition; D011487:Protein Conformation; D011489:Protein Denaturation; D051381:Rats; D013696:Temperature; D013710:Tendons / Q000166:cytology* / Q000502:physiology*
D003094:Collagen