Keratins are highly attractive natural biomaterials for medical applications due to their inherent self-assembly characteristics and biocompatibility. In this study, the molecular mechanism of rabbit hair keratin (RHK) gelation during cryogelation is investigated and the influence of cryogelation parameters on the gelation of keratin is systematically evaluated. Re-xidation of free cysteine thiols and formation of hydrogen bond are determined to be the main stabilizing forces in self-assembly of RHK gel, and ionic bonds are found to affect the uniformity of keratin hydrogels. pH affects the gelation by changing the electrostatic interaction between keratin molecules. Keratin will accumulate when pH is too low, but the stability of keratin hydrogels becomes worse when the pH is too high. With successive freezing–thawing (FT) cycles, the storage modulus of RHK cryogels substantially improved from 240.66 Pa at FT cycle 3 to 2483.3 Pa at FT cycle 9. Maintaining the balance of the interactive force between keratin molecules and between keratin molecules and water molecules is the basis of preparing uniform and stable keratin hydrogels.

中文翻译：

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冷冻消融制备兔毛角蛋白水凝胶的分子机制

由于其固有的自组装特性和生物相容性，角蛋白是非常有吸引力的医疗应用天然生物材料。本研究研究了冷冻凝胶化过程中兔毛角蛋白 (RHK) 凝胶化的分子机制，并系统评估了冷冻凝胶化参数对角蛋白凝胶化的影响。游离半胱氨酸硫醇的再氧化和氢键的形成被确定为 RHK 凝胶自组装的主要稳定力，并且发现离子键影响角蛋白水凝胶的均匀性。pH 通过改变角蛋白分子之间的静电相互作用来影响凝胶化。pH 值过低时角蛋白会积聚，但pH 值过高时角蛋白水凝胶的稳定性会变差。随着连续的冻融 (FT) 循环，