太赫兹时域光谱表征葡萄糖胺和胶原结晶

Changcheng Shi, Dongshan Wei, Chun-lei Du, Hongliang Cui, Yuting Ma
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引用次数: 0

摘要

太赫兹时域光谱(THz-TDS)已被证明是一种很有前途的固态分析工具,可以通过晶格振动来探测分子间的相互作用。然而,目前的研究通常是研究两个相对低分子量的生物或药物分子之间的相互作用。结晶过程中生物小分子与生物大分子的相互作用尚未见报道。在本研究中,THz-TDS作为表征结晶过程中生物小分子(氨基葡萄糖)和生物大分子(胶原蛋白)相互作用的新技术。质量比为1:1的溶剂混合样品中没有太赫兹吸收峰,说明葡萄糖胺的结晶过程受到了胶原蛋白的干扰。在质量比为7:1的溶剂混合样品中,太赫兹吸收峰的出现可能与葡萄糖胺与胶原蛋白相互作用的饱和有关。实验证实,溶解和冻干工艺对葡萄糖胺的结晶几乎没有影响。该研究进一步证明了THZ-TDS具有表征固体状态下生物小分子与生物大分子相互作用的能力。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Characterization of Glucosamine and Collagen crystallization by terahertz time-domain spectroscopy
Terahertz time-domain spectroscopy (THz-TDS) has been demonstrated as a promising solid-state analytical tool which can probe intermolecular interactions through crystal lattice vibrations. However, the current studies commonly investigate the interactions between two biological or pharmaceutical molecules with relatively low molecular weights. The interaction between small biomolecule and biomacromolecule in the crystallization process has not been reported. In this study, THz-TDS was used as a novel technique to characterize the interaction between small biomolecule (Glucosamine) and biomacromolecule (Collagen) in the crystallization process. The absence of THz absorption peak in solvent mixed sample with weight ratio of 1:1 showed the crystallization process of glucosamine was disturbed by collagen. The recurrence of THz absorption peak in solvent mixed sample with weight ratio of 7:1 may be related to the saturation of interaction between glucosamine and collagen. The dissolving and lyophilizing processes were validated to hardly affect the crystal formation of glucosamine. This study further demonstrates THZ-TDS has the capability to characterize the interaction between small biomolecule and biomacromolecule in solid-state.
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