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Synchrotron FTIR (S-FTIR) microspectroscopy was used to monitor the silk protein conformation in a range of single natural silk fibers (domestic and wild silkworm and spider dragline silk). With the selection of suitable aperture size, we obtained high-resolution S-FTIR spectra capable of semiquantitative analysis of protein secondary structures. For the first time, we have determined from S-FTIR the β-sheet content in a range of natural single silk fibers, 28 ± 4, 23 ± 2, and 17 ± 4% in Bombyx mori, Antheraea pernyi, and Nephila edulis silks, respectively. The trend of β-sheet content in different silk fibers from the current study accords quite well with published data determined by XRD, Raman, and (13)C NMR. Our results indicate that the S-FTIR microspectroscopy method has considerable potential for the study of single natural silk fibers.

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Usually, regenerated silk fibroin (RSF) hydrogels cross-linked by chemical agents such as horseradish peroxide (HRP)/HO perform elastic properties, while display unsatisfactory strength for practical applications especially as load-bearing materials, and inadequate stability when incubated in a simulated in vivo environment. Here, the RSF hydrogel with both excellent strength and elasticity was prepared by inducing the conformation transition from random coil to β-sheet in a restricted RSF network precross-linked by HRP/HO. Such "dual-networked" hydrogels, regarding the one with 10 wt % RSF (Mw: 220 kDa) as a representative, show around 100% elongation, as well as the compressive modulus and tensile modulus up to 3.0 and 2.5 MPa respectively, which are much higher than those of physically cross-linked natural polymer hydrogels (commonly within 0.01-0.1 MPa at the similar solid content). It has been shown that the enhanced comprehensive mechanical properties of RSF hydrogels derive from the formation of small-sized and uniformly distributed β-sheet domains in the hydrogel during the conformation transition of RSF whose size is limited by the first network formed by cross-linkers with HRP/HO. Importantly, the tough RSF hydrogel changes the normally weak recognition of various RSF hydrogels and holds a great potential to be the material in biomedical field because it seems to be very promising regarding its biocompatibility, biodegradability, etc.