Spectroscopic study of the effect of laser heating on collagen stability: Implications for tissue welding

Ward Small IV; Luiz B. Da Silva; Dennis L Matthews

doi:10.1117/12.312298

Spectroscopic study of the effect of laser heating on collagen stability: Implications for tissue welding

Ward Small IV, Luiz B. Da Silva, Dennis L Matthews

Research output: Chapter in Book/Report/Conference proceeding › Conference contribution

3 Scopus citations

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	https://doi.org/10.1117/12.312298
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/Territory	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

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10.1117/12.312298

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

Small IV, W, Da Silva, LB & Matthews, DL 1997, Spectroscopic study of the effect of laser heating on collagen stability: Implications for tissue welding. in RR Anderson, KE Bartels, LS Bass & CG Garrett (eds), Proceedings of SPIE - The International Society for Optical Engineering. vol. 3245, pp. 276-281, Lasers in Surgery: Advanced Characterization, Therapeutics, and Systems VIII, San Jose, CA, United States, 1/24/98. https://doi.org/10.1117/12.312298

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title = "Spectroscopic study of the effect of laser heating on collagen stability: Implications for tissue welding",

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. ",

keywords = "Cornea, Dehydration, Denaturation, Fourier transform infrared spectroscopy, Temperature feedback",

author = "{Small IV}, Ward and {Da Silva}, {Luiz B.} and Matthews, {Dennis L}",

year = "1997",

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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.

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KW - Dehydration

KW - Denaturation

KW - Fourier transform infrared spectroscopy

KW - Temperature feedback

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ER -

Spectroscopic study of the effect of laser heating on collagen stability: Implications for tissue welding

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