Structural changes of Bombyx mori fibroin from silk gland to fiber as evidenced by Terahertz spectroscopy and other methods.

Here we investigated the structural changes of silk fibroin during Bombyx mori silkworm spinning and reconstitution process. X-ray diffraction, Fourier transform infrared spectroscopy, polarized optical microscopy, and terahertz (THz) spectroscopy were applied to monitor the structural features of silk fibroin from posterior, middle silk glands, to cocoons, and then to reconstituted silk. Results show that from silk gland to cocoon, fibroin experiences a significant transformation in crystal structure from a typical silk I, to a silk I-rich mixed structure, and finally to a typical silk II state, accompanied with a change in secondary structure from α-helix and random coil structures to preferential orientation β-sheets. Compared with natural silk fibroins, the reconstituted silk fibroin lacks β-sheet conformation and orientation crystallization. Terahertz spectroscopy readily follows these silk fibroin structural changes. Two characteristic peaks for silk fibroin is observed in 2-10 THz. Their strength ratio is strongly correlated with the β-sheet conformation. The absorbance properties in 0.2-2.0THz also significantly change as a function of changing their crystal structures caused by diverse sources. All of these observations will help in the study of overall structure in silk fibroin to understand more completely the fibroin assembly process in natural spinning and reconstitution process.