Lu Shenzhou, Li Jiaojiao, Zhang Shanshan, Yin Zhuping, Xing Tieling, Kaplan David L
National Engineering Laboratory for Modern Silk, College of Textile and Clothing Engineering, Soochow University, Suzhou 215123, P. R. China.
J Mater Chem B. 2015 Apr 7;3(13):2599-2606. doi: 10.1039/c4tb01873g. Epub 2015 Feb 24.
The present study examines the influence of the hydrophilic-lipophilic environment, mediated by small molecules, on the structural changes in silk protein fibroin. Small molecules mediate the various hydrophilic-lipophilic balances (HLBs) that impact the organisation of silk protein chains. Changes in the silk fibroin structure due to additives are related to the HLB value. At HLB > 10, silk fibroin primarily forms Silk I crystalline structures. Small molecules with HLB < 8.9 primarily induce the formation of Silk II crystalline structures. When 8.9 < HLB < 10, the crystalline structure of silk is related to the content of small molecules. The Silk I structure is primarily formed when the content of small molecules is low, whereas the Silk II structure is formed when the small molecule content is high. The structure of silk fibroin is maintained by regulating the HLB in the fibroin environment. This type of control for the functional design of materials may play a role in fine-tuning the biomaterial properties of silk fibroin protein.
本研究考察了由小分子介导的亲水性-亲脂性环境对丝蛋白纤维结构变化的影响。小分子介导各种亲水性-亲脂性平衡（HLB），这些平衡会影响丝蛋白链的组织。添加剂导致的丝素蛋白结构变化与HLB值有关。当HLB>10时，丝素蛋白主要形成丝I晶体结构。HLB<8.9的小分子主要诱导丝II晶体结构的形成。当8.9<HLB<10时，丝的晶体结构与小分子含量有关。小分子含量低时主要形成丝I结构，而小分子含量高时形成丝II结构。通过调节丝素蛋白环境中的HLB来维持丝素蛋白的结构。这种对材料功能设计的控制方式可能在微调丝素蛋白生物材料性能方面发挥作用。
