Abstract
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 Au3+ 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). The in situ prepared GY-14@Au NPs were utilized as a built-in colorimetric indicator. The influences of specified physiological factors including decreasing the pH, the addition of calcium ions and isopropanol treatment on the self-assembly behavior of GY-14@Au NPs in aqueous solution have been studied. On the basis of transmission electron microscopy (TEM), dynamic light scattering (DLS), atomic force microscopy (AFM), Fourier transform infrared (FT-IR) spectroscopy and circular dichroism (CD) measurements, the color changes and the UV-Vis absorption peak shift of GY-14@Au NPs were attributed to the conformational change of the GY-14 peptide. The colorimetric readout can be seen with the naked eye, providing an efficient indicator to study the conformational changes of peptides exposed to various environmental stimuli.
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