| 초록 |
PMAP-23 has potent antimicrobial activity. The amidation of the carboxyl terminus of the peptide generally enhances the structural stability and antimicrobial activity or decreases cytotoxicity. The antibacterial activity of two peptides, PMAP-23C with a free C-terminus and PMAP-23N with an amidated C-terminus, was similar against gram-negative bacteria due to similar neutralization activity of Lipopolysaccharide. However, PMAP-23N was in an anti-parallel orientation across the outer to inner leaflet of the bacterial inner membrane, while PMAP-23C was orientated parallel to the lipid bilayer. These results suggest that the N-terminal amidation of PMAP-23 provide structural stability and increase the cationic charge following translocation into the bacterial inner membrane. |
