ABSTRACT
Bis-lentivirus lytic protein 1 (Bis-LLP1) and polymyxin B exhibited similar killing activities against Serratia marcescens. By electron microscopy, bis-LLP1 interacted with the outer and cytoplasmic bacterial membranes, while polymyxin B affected only the outer membrane. The results of standard biochemical probes supported the findings of the electron microscopy studies, suggesting that these antimicrobial peptides have different mechanisms of action.
Unique Functional Properties of Conserved Arginine Residues in the Lentivirus Lytic Peptide Domains of the C-terminal Tail of HIV-1 gp41