Effect of Net Positive Charge and Charge Distribution on the Polar Face of Amphipathic α-Helical Antimicrobial Peptides on their Biological and Biophysical Properties

摘要

This is a systematic study of varying the number of positively charged residues on the polar face of our amphipathic α-helical antimicrobial peptides, D1 and analogs D5 [1-5] and D17 to D22 (Table 1). The nonpolar face is identical in the six analogs D17 to D22. As shown in Table 1, the number of lysine residues increases systematically from 4 (D17), 5 (D18), 6 (D19), 7 (D20), 8 (D21) to 9 (D22) on the polar face. The net charge on the peptides concomitantly increases from +5 to +10 because of the specificity determinant on the nonpolar face, K13, in each analog.