Flexibility regeneration of silk fibroin in vitro.
Although natural silk fibers have excellent strength and flexibility, the regenerated silk materials generally become brittle in the dry state. How to reconstruct the flexibility for silk fibroin has bewildered scientists for many years. In the present study, the flexible regenerated silk fibroin films were achieved by simulating the natural forming and spinning process. Silk fibroin films composed of silk I structure were first prepared by slow drying process. Then, the silk fibroin films were stretched in the wet state, following the structural transition from silk I to silk II. The difference between the flexible film and different brittle regenerated films was investigated to reveal the critical factors in regulating the flexibility of regenerated silk materials. Compared with the methanol-treated silk films, although having similar silk II structure and water content, the flexible silk films contained more bound water rather than free water, implying the great influence of bound water on the flexibility. Then, further studies revealed that the distribution of bound water was also a critical factor in improving silk flexibility in the dry state, which could be regulated by the nanoassembly of silk fibroin. Importantly, the results further elucidate the relation between mechanical properties and silk fibroin structures, pointing to a new mode of generating new types of silk materials with enhanced mechanical properties in the dry state, which would facilitate the fabrication and application of regenerated silk fibroin materials in different fields.
National Engineering Laboratory for Modern Silk, College of Textile and Clothing Engineering, Soochow University, Suzhou 215123, People's Republic of China.
Cencen
C
Zhang
Dawei
D
Song
Qiang
Q
Lu
Xiao
X
Hu
David L
DL
Kaplan
Hesun
H
Zhu
D000818:Animals; D012831:Bombyx; D002152:Calorimetry, Differential Scanning; D003890:Desiccation; D005349:Fibroins / Q000737:chemistry* / Q000648:ultrastructure; D000432:Methanol / Q000737:chemistry; D049329:Nanostructures / Q000737:chemistry / Q000648:ultrastructure; D017433:Protein Structure, Secondary; D017550:Spectroscopy, Fourier Transform Infrared; D013718:Tensile Strength; D013818:Thermogravimetry; D014867:Water / Q000737:chemistry; D014961:X-Ray Diffraction
D014867:Water; D005349:Fibroins; D000432:Methanol