Regulating the structure of tyrosinase-crosslinking silk fibroin scaffolds
The structural controllability of silk fibroin scaffolds is a key fundamental topic in its biomedical applications.The tyrosinase-crosslinking silk fibroin (t-SF) scaffolds with varying reaction SF concentration were constructed to investigate the influence on the pore structure of SF scaffolds in this study.The FTIR results showed tyrosine residues react with the amino groups of SF to form inter-and intramolecular covalent bonds at the presence of tyrosinase.The conformation of t-SF scaffolds was unaffected by the reaction SF concentration, which was still mainly α-helix and random coil structure.Furthermore, with the concentration of SF increased, the average pore size reduced from 101 to 73 μm and the porosity decreased from 60 to 47% significantly.These results revealed that tyrosinase as agent could induce self-crosslinking of SF, and the pore structure of SF scaffolds could be regulated by adjusting the reaction SF concentration.
silk fibroin tyrosinase,crosslinking pore structure scaffolds
Yu Liu Yu-hong Jiao Ming-zhong Li
National Engineering Laboratory for Modern Silk, College of Textile and Clothing Engineering, Soochow University, Suzhou, china
国际会议
The 9th China International Silk Conference (ISC2016)(第九届中国国际丝绸会议)
广西宜州
英文
110-114
2016-09-09（万方平台首次上网日期，不代表论文的发表时间）