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 micrometer 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$+$MIN@1$/ indicated that conformational changes associated with denaturation occurred. Samples heated using a temperature feedback controlled 1.9 micrometer 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 degrees Celsius 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. !20
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机译：摘要：胶原蛋白被认为在激光组织焊接中起主要作用。此外，基本的融合机制可以包括胶原纤维的热变性。进行了激光加热（1.9微米二极管激光）对胶原蛋白构象影响的体外研究。获得了天然和加热的猪角膜的傅立叶变换红外光谱。在3320 cm $ + $ MIN @ 1 $ /附近的胶原蛋白A酰胺带发生低频移动，表明发生了与变性相关的构象变化。使用温度反馈控制的1.9微米二极管激光器加热的样品显示酰胺A峰频率随温度升高而逐渐降低，就像在水浴中加热的样品一样。对于两种加热方案，均在高于85摄氏度的温度下实现了完全变性。激光加热引起的水分流失可能会降低胶原蛋白多肽链的迁移率，并导致变性温度升高。 ！20
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