Abstract
The conformation transition from random coil and/or helix to β-sheet of silk
protein is the most important step in the formation of silk fiber in nature as well
as by artificial spinning. Time-dependent Fourier transform infrared (FT-IR)
spectroscopy was used in this research to monitor such a conformation transition
process induced by the organic solvents methanol, ethanol, propanol, isopropanol,
and acetone. The kinetics of β-sheet formation of regenerated Bombyx mori
silk fibroin in these organic solvents was obtained by the ∆absorbance-time curve
from the time-dependent difference infrared spectra. The results showed that the
conformation transition rate of silk fibroin was methanol > ethanol > acetone
> propanol > isopropanol, which is in accordance with the polarity of these
organic solvents. In connection with the mechanical properties and morphologies of
regenerated silk fibers using these organic solvents as coagulation bath reported in
the literature, we may conclude that the conformation transition rate of silk
protein in the organic solvent is very important in wet-spinning to produce
high-performance regenerated silk fibers.
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