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The histidine-rich antimicrobial peptides Gad-1 and Gad-2, from paralogous genes in cod, provide an opportunity to examine the effect of charge and nonelectrostatic factors on peptide-vesicle interaction and on peptide antimicrobial activity. In this study, the dependence of vesicle ζ-potential on peptide concentration has been used to examine the binding of these peptides to model vesicle surfaces at pH = 5.0, for which the charges of Gad-1 and Gad-2 are +8 and +5, respectively, and at pH = 7.0, where their charges are +3 and +1, respe
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