To assess the structure of the peptide, we performed molecular dynamics (MD) simulations in different solvents: wateran excellent proton donor/acceptor solvent; methanol (MeOH)a polar protic solvent that is a poor proton donor/acceptor; and chloroform (CHCl3)an aprotic solvent. The MD results (Fig. and Figure ) indicated that in MeOH, both the (EA)4 and (A)8 peptides (in their D-B-A configurations) adopt a mostly α-helical structure. In CHCl3, the (EA)4 peptide possesses less proportion of an α-helix structure, whereas the (A)8 peptide has a predominant α-helical structure. In water, the (A)8 peptide still has some percentage of an α-helical structure, but the (EA)4 peptide loses its structure. The results in water are supported by circular dichroism measurements (Figure ), which could be performed only for the D-B-A peptides in water due to the solvents' cut-off absorption.