Authors: Chen, Xin; Cai, Huifei; Ling, Shengjie; Shao, Zhengzhong; Huang, Yufang

Source: Applied Spectroscopy, Volume 66, Issue 6, Pages 156A-170A and 609-730 (June 2012) , pp. 696-699(4)

Publisher: Society for Applied Spectroscopy

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 Δabsorbance-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.

Keywords: Time-dependent FT-IR spectroscopy; Fourier transform infrared spectroscopy; Silk protein; Conformation transition; Organic solvent; Artificial spinning

Document Type: Research article

DOI: http://dx.doi.org/10.1366/11-06551

Affiliations: 1: State Key Laboratory of Molecular Engineering of Polymers, Department of Macromolecular Science, Laboratory of Advanced Materials, Fudan University, Shanghai, 200433, People's Republic of China

Publication date: 2012-06-01

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