Effect of pH on the Conformational Transition of Silk Fibroin in Aqueous Solution Monitored by Thioflavin-T Fluorescence.

In this work, the potential application of the fluorescence dye Thioflavin-T (ThT), which can specifically bind to amyloid, as a powerful tool for monitoring secondary structural transitions of silk fibroin (SF) induced by pH in low solution concentrations was examined. Results showed that ThT emission intensities substantially increased when pH decreased from 6.8 to 4.

Label-free Fluorescence Turn on Trypsin Assay Based on Gemini Surfactant/heparin/Nile Red Supramolecular Assembly.

In this research, we designed a label-free fluorometric turn-on assay for trypsin and inhibitor screening, based on a spherical cationic gemini surfactant ethylene-bis (dodecyl dimethyl ammonium bromide) (EDAB)/heparin/Nile red (NR) supramolecular assembly system. The introduction of gemini surfactant EDAB as template greatly enhanced its salt resistance and resulted in the supramolecular assemblies with diameters ranging from 20 to 100 nm. The fluorometric assay for trypsin was performed by firstly disassembling with protamine (a heparin-binding protein) and then re-assembling through hydrolysis of protamine.

Visible sensing of conformational transition in model silk peptides based on a gold nanoparticles indicator.

To understand protein structural transition and β-sheet formation is of importance in disparate areas such as silk protein processing and disease related β-amyloid behavior. Herein, GAGSGAGAGSGAGY (GY-14), a tetradecapeptide based on the crystallizable sequence of silk fibroin, was employed as a model peptide of the crystalline regions of silk fibroin. Due to the incorporation of tyrosine (Y), GY-14 was able to reduce Au to Au NPs and further stabilize them without any external reducing or capping reagents to produce GY-14 stabilized Au NPs (GY-14@Au NPs).

Stability and cytocompatibility of silk fibroin-capped gold nanoparticles.

Surface engineering is crucial in the colloidal stability and biocompatibility of nanoparticles (NPs). Protein silk fibroin (SF), which gained interest in biomaterial and regenerative medicine, was used in this study to stabilize gold (Au) NPs. Characterization results from UV-Vis spectroscopy revealed that SF-capped Au NPs (SF-Au NPs) possessed remarkable colloidal stabilities in the pH range of 2 to 11 and salt concentration range of 50mM to 1000 mM.