CD conformational and modeling studies of a synthetic peptide VPDLLADLLK in different media

CD spectral studies of VPDLLADLLK, a synthetic peptide shows that it undergoes a conformational transition from an unordered structure to a more ordered structure from a polar to a non-polar homogeneous medium. In microheterogeneous media like SDS, CTAB micelles and DMPC lipid bilayer, the peptide exhibits a more stable α- helical structure. The helical conformation is stabilized in DMPC lipid bilayer. Homology modeling gives the picture of α- helix, where the middle six residues LLADLL form the turns of the helix.