Figure 1.

Amino acid sequences of the three natural arenicins and three analogues studied in this work. The color coding is as follows: blue, differences in primary structure of natural arenicins, taking Ar-1 as the reference; red, amino acid substitutions or deletions (indicated by the “–” symbol) in Ar-1[V8R] and ALP1 compared to Ar-1; purple, amino acid substitutions in AA139 compared to Ar-3. Cysteine residues are highlighted in yellow. Two invariant cysteines are involved in the disulfide bond common to all arenicin peptides and are shown by the solid black line in the upper part; the disulfide bond shared only by Ar-3 and its analogue, AA139, is shown by the dashed line in the bottom. All peptides have an unmodified amine and carboxyl at the N- and C-terminus, respectively. Some physicochemical properties of the peptides (net charge at pH 7.0 and hydrophobicity as the GRAVY index) are shown on the right.