It has previously been established that various RADA16-I peptides assemble into stable β-sheet structures . Circular dichroism was used as one of the tools for conformational examination of the studied peptide hybrids. The samples were incubated to form gels and then diluted to appropriate concentrations. All spectra of the synthesized peptides gave positive bands around 196 nm and a negative band at 218 nm, which indicated the presence of a β-sheet conformation, the same as in the original RADA16-I. However, the CD spectra show a decrease in the intensity of molar ellipticity between peptides (Fig. ), which means a lower ratio of β-sheet formation in the hybrid peptides. We subsequently examined the thermal stability of the RADA hybrids using CD. Figure In the next step, analysis was carried out to confirm the presence of β-structures that form a complex with thioflavin T (ThT). This technique, which is used to detect amyloid fibrils, has successfully been applied to image RADA16-I nanofibers . Fig. demonstrates that thioflavin T formed a complex with the studied RADA fibres, which was indicated by fluorescence intensity at 482 nm. The differences between the fluorescence intensities reflected different ratios of formation of β-sheets.