Abstract
Collagen is believed to play a major role in laser tissue welding. Furthermore, the fundamental fusion mechanism(s) may include thermal denaturation of the collagen fibers. An in vitro investigation of the effect of laser heating (1.9 μm diode laser) on collagen conformation was performed. Fourier transform infrared (FTIR) spectra of native and heated porcine cornea were obtained. A low-frequency shift in the amide A band of collagen around 3320 cm -1 indicated that conformational changes associated with denaturation occurred. Samples heated using a temperature feedback controlled 1.9 μm diode laser showed a gradual decrease in the amide A peak frequency with increasing temperature, as did samples heated in a water bath. Complete denaturation was achieved at temperatures above 85°C for both heating protocols. Water loss induced by laser heating may have reduced the mobility of the collagen polypeptide chains, and contributed to the elevated denaturation temperature.
Original language | English (US) |
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Title of host publication | Proceedings of SPIE - The International Society for Optical Engineering |
Editors | R.R. Anderson, K.E. Bartels, L.S. Bass, C.G. Garrett |
Pages | 276-281 |
Number of pages | 6 |
Volume | 3245 |
DOIs | |
State | Published - 1997 |
Externally published | Yes |
Event | Lasers in Surgery: Advanced Characterization, Therapeutics, and Systems VIII - San Jose, CA, United States Duration: Jan 24 1998 → Jan 25 1998 |
Other
Other | Lasers in Surgery: Advanced Characterization, Therapeutics, and Systems VIII |
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Country | United States |
City | San Jose, CA |
Period | 1/24/98 → 1/25/98 |
Keywords
- Cornea
- Dehydration
- Denaturation
- Fourier transform infrared spectroscopy
- Temperature feedback
ASJC Scopus subject areas
- Electrical and Electronic Engineering
- Condensed Matter Physics