Experimental study of the effect of temperature on collagen conformational changes in skin tissue welded by femtosecond laser

Huang, Jun; Xia, Shengnan; Jia, Mo-Ran; Chen, Yuxin; Li, Jincheng; Wang, Kehong; Menemenlis, Dimitris

doi:10.1016/j.ijleo.2023.171184

Cited by 2 publications

(2 citation statements)

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“…When the femtosecond laser welds the skin tissue, as the temperature rises, the collagen in the skin gradually de‐helixation and forms a new collagen triple helix structure, and when the temperature is high, water is gradually lost from the skin tissue, resulting in carbonization. The spectral intensity of different characteristic peaks and changes in the secondary structure of proteins in Raman spectroscopy can reflect the degree of denaturation of proteins and describe the degree of thermal damage to skin tissues [23]. The femtosecond laser‐welded skin samples of the 5th, 7th, 9th, and 13th group of tests were selected from Table 1 for analyzing the changes in the secondary structure of proteins by Raman spectroscopy, and for analyzing the correspondence between the degree of thermal denaturation and the degree of denaturation of the skin tissue proteins.…”

Section: Results Analysismentioning

confidence: 99%

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Effect of femtosecond laser process parameters on the thermal denaturation degree of skin tissue

Huang,

Jia,

Xia

et al. 2024

Journal of Biophotonics

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The influence of femtosecond laser parameters on the degree of thermal denaturation was studied experimentally. The relationship between the degree of thermal denaturation and the characteristic parameters of skin microstructure and the secondary structure of skin tissue proteins in characterizing the degree of thermal damage was analyzed. The results showed the interaction of laser power, laser power, and scanning speed had a significant effect on the degree of thermal denaturation; greater degrees of thermal denaturation were associated with larger second‐order moments of the texture angle of the skin microtissue and smaller entropy values and contrast, indicating a greater degree of thermal damage; and higher peak temperature, the lower peak intensity of Raman spectra, decrease in the percentage area of α‐helix fitted curves and increase in the percentage area of β‐sheet and β‐turn fitted curves indicate that the protein is denatured to a large extent that means thermal damage is large.

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Section: Results Analysismentioning

confidence: 99%

“…However, there is a significant difference in spectral intensity, which decreases with increasing peak temperature. The lower peak intensity of the spectra indicated that the degree of protein denaturation increased with the increase in temperature [23].…”

Section: Results Analysismentioning

confidence: 99%