Obtained peptides were used for further analysis via NMR and CD. The CD spectra of the TMC.HSV peptide in the highest concentration of DPC or POPC had a maximum band at about 190 nm and two minima at wavelengths of about 204 nm and 222 nm, which is characteristic of an α-helix structure (Figure ). In the case of CD spectra measured for the TMC.HSV peptide in DPC, it can be seen that even at low concentration of DPC peptide forms stable helical structure. In water or at a low concentration of POPC, the structure of the TMC.HSV peptide is unordered but starts to form a helical structure at higher concentrations of POPC, but only at 0.5 mM POPC forms a stable α-helix. For the TMC.HSV peptide, the mean molar ellipticity values (Δε) decrease with increasing concentration of POPC at a wavelength about 210 nm and shift towards higher wavelength values (Figure ). It also means that TMC.HSV peptide takes the shape of a stable α-helix at high concentration of POPC.