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. Author manuscript; available in PMC: 2019 Oct 8.
Published in final edited form as: Adv Exp Med Biol. 2019;1117:241–255. doi: 10.1007/978-981-13-3588-4_13

Figure 2.

Figure 2

Saturation-dependent activity of an antimicrobial peptide and its inhibition by host cells. The protease resistant AMP D-ARVA (rrgwalrlvlay-NH2) was used in these experiments1–3. A: Measured binding of D-ARVA to E. coli cells. B: Measured binding of D-ARVA to human RBCs. C: Experimental measurements compared to simulation of a mixed experiment assuming simple competition between E. coli and RBC shows that the measured binding accounts for the loss of activity when host cells are present. D: Survival of different innocula of E. coli incubated with 20 μM D-ARVA in conjunction with the binding curve in panel A, enables comparison of peptide lethality and the number of peptides bound to each bacterial cell. More than 2×108 peptides bound per cell are required for sterility.