| 초록 |
The spinning process, i.e. the supramolecular structural transition of silk fibroin in the aqueous environment of a gland, remains poorly understood. In efforts to elucidate the processes involved, self-assembly of many natural proteins such as silk fibroin has been the focal point of a significant body of research over the past few decades as scientists have strived to discover fundamental rules of nature and develop new engineering applications. In the present study, the change of the supramolecular structure of silk fibroin from Bombyx mori silkworm as a function of pH was characterized. A transition from spherical micelles to nanofibrils was observed in dilute aqueous solution of the protein with a pH reduction. The morphologies were assessed by transmission electron microscopy and the secondary structure of the silk fibroin was characterized by circular dichorism spectroscopy. |
