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) |
|---|---|
| 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 |
|---|---|
| Country | United States |
| City | San Jose, CA |
| Period | 1/24/98 → 1/25/98 |
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Keywords
- Cornea
- Dehydration
- Denaturation
- Fourier transform infrared spectroscopy
- Temperature feedback
ASJC Scopus subject areas
- Electrical and Electronic Engineering
- Condensed Matter Physics
Cite this
Spectroscopic study of the effect of laser heating on collagen stability : Implications for tissue welding. / Small IV, Ward; Da Silva, Luiz B.; Matthews, Dennis L.
Proceedings of SPIE - The International Society for Optical Engineering. ed. / R.R. Anderson; K.E. Bartels; L.S. Bass; C.G. Garrett. Vol. 3245 1997. p. 276-281.Research output: Chapter in Book/Report/Conference proceeding › Conference contribution
}
TY - GEN
T1 - Spectroscopic study of the effect of laser heating on collagen stability
T2 - Implications for tissue welding
AU - Small IV, Ward
AU - Da Silva, Luiz B.
AU - Matthews, Dennis L
PY - 1997
Y1 - 1997
N2 - 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.
AB - 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.
KW - Cornea
KW - Dehydration
KW - Denaturation
KW - Fourier transform infrared spectroscopy
KW - Temperature feedback
UR - http://www.scopus.com/inward/record.url?scp=0031289665&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0031289665&partnerID=8YFLogxK
U2 - 10.1117/12.312298
DO - 10.1117/12.312298
M3 - Conference contribution
AN - SCOPUS:0031289665
VL - 3245
SP - 276
EP - 281
BT - Proceedings of SPIE - The International Society for Optical Engineering
A2 - Anderson, R.R.
A2 - Bartels, K.E.
A2 - Bass, L.S.
A2 - Garrett, C.G.
ER -