A study on the flow stability of regenerated silk fibroin aqueous solution.
The flow stability of silk fibroin (SF) aqueous solutions with different concentrations under different temperatures was investigated. It was found that the flow stability decreased quickly with the increase of solution concentration and temperature. X-ray diffraction, Fourier transform infrared (FTIR) and Raman spectroscopy analysis showed that silk fibroin in aqueous solution was mainly in random coil and alpha-helix conformation. However, it turned into alpha-helix and beta-sheet conformation after gelation, and both silk I and silk II crystalline structures appeared accordingly. The investigation implies that the original dilute regenerated SF aqueous solution should be stored under low temperature and concentrated just before spinning.
Wang
Hong
H
State Key Laboratory for Modification of Chemical Fibers and Polymer Materials, College of Material Science and Engineering, Donghua University, Shanghai 200051, PR China.
Zhang
Yaopeng
Y
Shao
Huili
H
Hu
Xuechao
X
D004305:Dose-Response Relationship, Drug; D005349:Fibroins / Q000737:chemistry*; D046911:Macromolecular Substances / Q000737:chemistry; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D047011:Silk / Q000737:chemistry* / Q000378:metabolism; D017550:Spectroscopy, Fourier Transform Infrared; D013059:Spectrum Analysis, Raman; D013696:Temperature; D013997:Time Factors; D014867:Water / Q000737:chemistry; D014961:X-Ray Diffraction
D046911:Macromolecular Substances; D047011:Silk; D014867:Water; D005349:Fibroins