[Spectroscopic study on the conformational change of silk fibroin in methanol-water mixtures].

A combinational study of circular dichroism, intrinsic fluorescence of protein and exogenous fluorescence probe of ANS was made to investigate the conformational change of silk fibroin in methanol-water mixtures as well as the mechanism. The spectral results showed that small hydrophobic regions were formed in silk fibroin in methanol-water mixtures at the concentration lower than 30% (V/V) via hydrophobic interaction, which was decreased at higher methanol content due to a structural transition of silk fibroin from random coil to beta-sheet. The conformational change of silk fibroin was found to be of a close relationship with the microstructure of the solvent and to be determined by the interaction between the peptide unit of silk fibroin and the cluster of the mixed solvent.