Surface analysis of novel fibroin films based on well-preserved crystalline structures

Abstract

We recently reported that a highly homogeneous aqueous suspension of fibroin nanofiber (FNF) can be simply obtained by mechanical water-grinding a heterogeneous aqueous fibroin slurry and that the FNF in the suspension preserves the native β-sheet secondary structure during this mechanical treatment. The current study reports the surface properties of well-preserved crystalline structure novel FNF film from water-grinding preparation as compared with those of typical, conventionally prepared regenerated fibroin (RF) film. RF film was not treated with alcoholic solutions and was verified to be amorphous from a WAXD diffraction diagram. The air-side surfaces of the FNF semi-crystalline and RF amorphous films were studied to clarify differences using scanning electron microscopy (SEM), atomic force microscopy (AFM), attenuated total reflection Fourier transform infrared spectroscopy (ATR-FTIR), static water contact angle, and X-ray photoelectron spectroscopy (XPS). The well-preserved crystalline in the FNF film was found to exist near a slightly deep surface region and to act as a physically cross-linking domain, governing the molecular motions of the amorphous polypeptide chains at the very shallow surface region.