Thermal denaturation is the primary reason for the loss of excellent performance for collagen-based materials. It is particularly urgent to explore an effective structure restoration strategy for thermally denatured collagen. In this study, three different degrees of collagen thermal denaturation models were constructed; the effects of ultrahigh pressure treatments of varying intensities on the structure and properties of partially thermal denatured collagen were investigated. Those results showed that ultrahigh pressure partially restores the triple helix conformation and the α helix of low thermally denatured collagen molecules and moderately restores collagen thermal stability. However, this recovery is not a “perfect” structural restoration; it cannot effectively restore the fibrotic ability of collagen which leads to a decrease in the fiber diameter of the product and an increase in the storage modulus of the product gel. As the degree of thermal denaturation of collagen increases, the ultrahigh pressure recovery effect is gradually lost. For moderate thermally denatured collagen, ultrahigh pressure treatments only recover a small amount of its triple helical conformation. For high thermally denatured collagen, ultrahigh pressure treatments exacerbate the destruction of the three-dimensional structure of collagen molecules, thereby losing the order of molecular structure and the capability of fibrosis self-assembly.

中文翻译：

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超高压处理恢复热变性胶原蛋白的结构

热变性是胶原基材料失去优异性能的主要原因。探索热变性胶原蛋白的有效结构恢复策略尤为紧迫。在这项研究中，构建了三种不同程度的胶原蛋白热变性模型。研究了不同强度的超高压处理对部分热变性胶原蛋白的结构和性能的影响。这些结果表明，超高压部分地还原了低热变性胶原分子的三螺旋构象和α螺旋，并适度地还原了胶原的热稳定性。但是，这种恢复并不是“完美”的结构恢复；它不能有效地恢复胶原蛋白的纤维化能力，从而导致产品的纤维直径减小和产品凝胶的储能模量增加。随着胶原蛋白的热变性程度的增加，超高压恢复作用逐渐消失。对于中等程度的热变性胶原蛋白，超高压处理只能恢复少量的三重螺旋构象。对于高热变性胶原蛋白，超高压处理加剧了胶原蛋白分子三维结构的破坏，从而失去了分子结构的顺序和纤维化自组装的能力。超高压恢复效果逐渐消失。对于中等程度的热变性胶原蛋白，超高压处理只能恢复少量的三重螺旋构象。对于高热变性胶原蛋白，超高压处理加剧了胶原蛋白分子三维结构的破坏，从而失去了分子结构的顺序和纤维化自组装的能力。超高压恢复效果逐渐消失。对于中等程度的热变性胶原蛋白，超高压处理只能恢复少量的三重螺旋构象。对于高热变性胶原蛋白，超高压处理加剧了胶原蛋白分子三维结构的破坏，从而失去了分子结构的顺序和纤维化自组装的能力。