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利用太赫兹时域光谱技术测量固体胶原蛋白25～120℃加热变性过程中的吸收谱和折射率谱,发现其吸收率及折射率逐渐减小,变性后返回室温时的测量结果与120℃时非常接近。又利用一阶Debye模型拟合胶原蛋白加热变性过程的介电谱,发现弛豫时间随着温度的升高而逐渐变大。因此认为胶原蛋白的加热变性是构象渐变过程。同时,弛豫时间随温度的变化满足Arrihenius方程,拟合得到的活化能为5.53 kJ/K.mol,可定量表征胶原蛋白加热变性过程的难易程度。结果证明利用太赫兹时域光谱技术可以检测固体蛋白质类药物的温度稳定性。
The absorption spectrum and refractive index spectrum of solid collagen were measured by terahertz time-domain spectroscopy in the process of heat-denatured from 25 to 120 ℃. The absorbance and refractive index of solid collagen decreased gradually. When measured at 120 ℃ very close. The first-order Debye model was also used to fit the dielectric spectra of collagen during heat-denaturation process. It was found that the relaxation time gradually increased with the increase of temperature. Therefore, it is considered that the heat denaturation of collagen is a conformational gradual change process. At the same time, the change of relaxation time with temperature satisfies the Arrihenius equation, and the activation energy of fitting is 5.53 kJ / K.mol, which can quantitatively characterize the degree of easiness of heating and degeneration of collagen. The results demonstrate the use of terahertz time-domain spectroscopy to detect the temperature stability of solid protein drugs.