Silk fibroin is a natural polymer with a unique repetitive structure that translates to extraordinary properties in terms of processability and mechanical properties. The Bombyx mori silk has a molecular weight of ∼415 kDa and consists of a light chain and a heavy chain. Its heavy chain is organized into 12 crystalline domains. Each of these crystalline domains contains subdomains of ∼70 amino acid containing blocks. It is well understood that the heavy chain of the protein is responsible for its processing versatility and excellent mechanical properties; however, the need for the high number of monomeric repeating units is unclear, and the individual properties of crystalline regions compared to those of the full-length protein are not understood. The work described herein assessed the possibility of using recombinant crystalline regions as alternative biomaterials for applications such as tissue adhesives. Our results indicate that while the two tested substructures do not fully recapitulate the native silk fibroin’s properties, they appear to be a suitable alternative for the production of silk-based medical adhesives.

中文翻译：

---

重组丝素结晶区域作为全长蛋白质的生物材料替代品

丝素蛋白是一种天然聚合物，具有独特的重复结构，在加工性能和机械性能方面具有非凡的性能。在家蚕蚕丝的分子量约为 415 kDa，由轻链和重链组成。它的重链被组织成 12 个晶体结构域。这些晶体结构域中的每一个都包含含有约 70 个氨基酸的块的子结构域。众所周知，蛋白质的重链是其加工多功能性和优异机械性能的原因；然而，对大量单体重复单元的需求尚不清楚，与全长蛋白质相比，结晶区域的个体特性尚不清楚。本文描述的工作评估了使用重组晶体区域作为替代生物材料用于组织粘合剂等应用的可能性。