Figure 3.

(A) Overall scheme of the most common interactions between antiviral peptides with an influenza virus lipid bilayer. Due to electrostatic interactions positively charged peptides are attracted by lipid bilayer with negative charge. The peptides insert into lipid bilayer (I.). The critical concentration of peptides triggers the lipid bilayer disruption. These phenomenon results in formation of artificial pores (II.) through which the low mass molecules penetrate into the capsid and contribute to the lipid bilayer destruction and leakage of viral components (III.) as well as disruption of NA and HA functions (IV.); (B) Scheme of function of polymerase assembly in virus replication cycle. Antiviral peptides may bind to PB2 subunit (peptides derived from PB1 subunit) and thus prevent the assembly of influenza polymerase complex via blocking of active binding site of PB2 subunit.