Conformational Analysis of Ramosin Peptide

The analysis of the conformation of the Ramosin peptide was performed through circular dichroism (CD). CD spectroscopy was carried out on a JASCO J-815 CD Spectrometer (JASCO Corp., Tokyo, Japan) in the far ultraviolet (UV) range (190–250 nm), using quartz cuvettes (0.1 cm path length). Each CD spectra of the synthetic peptide was recorded, averaging three scans in continuous scanning mode. Solvent blank was subtracted from each sample spectrum. Molar ellipticity was calculated for each spectra using 250 µL of 2 mM peptide in 30% (v/v) 2,2,2-trifluoroethanol (TFE), water, phosphate buffered saline (PBS) 2 mM pH = 7.4, sodium bicarbonate buffer 1 M pH = 8.5, and sodium acetate 3 M pH = 5. Resulting data were analyzed using Spectra Manager software (Version 2.0, JASCO Corp., Tokyo, Japan) [41 (link),42 (link)].