| 초록 |
Silk fiber, secreted by silkworm is composed of two structural proteins, fibroin(SF) and sericin(SS). SF is a fibrous protein that consists of heavy and light chain linked by disulfide bond. The twin thread of SF is covered with glue like layer of SS. SF is synthesiszed in the posterior gland and immigrated into the middle gland. SS is synthesized in the middle gland and stored with fibroin until spinning. The secret of silk spinning mechanism lies on the stability of SF in the middle gland until spinning. In the present study, the effect of pH on the conformational structure and interfacial interaction of SF and SS was investigated, because the pH of silk gland varied from near neutral in the posterior division to weakly acidic condition in the anterior division. In order to mimic the structure of silk proteins, we made the phase separated condition between SF and SS. The gelation time and conformational change of SF was observed in the presence of SS according to the pH changes. |
