Interaction mode of a symmetric Trp-rich undeca peptide PST11-RK with lipid bilayers.
To better understand the mode of action of the antimicrobial peptide PST11-RK, we investigated its (1) bactericidal kinetics, (2) ability to induce bacterial membrane depolarization, (3) ability to bind to liposomes, (4) cis/trans prolyl isomerization, (5) lipid binding kinetics and (6) translocation across lipid bilayers. Our findings suggest that PST11-RK acts mainly by collapsing the cytoplasmic membrane potential; it first attaches to the membrane via cationic C- and N-terminal residues and then inserts its central hydrophobic residues into the lipid interior. In addition, it seems likely that cis/trans isomerization facilitates the translocation of PST11-RK across the lipid bilayer, where it may interact with secondary intracellular targets.
Yang
Sung-Tae
ST
Department of Life Science, Gwangju Institute of Science and Technology, Gwangju, South Korea.
Shin
Song Yub
SY
Kim
Jae Il
JI
D000890:Anti-Infective Agents / Q000737:chemistry* / Q000494:pharmacology; D004926:Escherichia coli / Q000254:growth & development; D057927:Hydrophobic and Hydrophilic Interactions; D007536:Isomerism; D007700:Kinetics; D008051:Lipid Bilayers / Q000737:chemistry*; D008564:Membrane Potentials / Q000187:drug effects; D009842:Oligopeptides / Q000737:chemistry* / Q000494:pharmacology; D011485:Protein Binding; D021381:Protein Transport; D013211:Staphylococcus aureus / Q000254:growth & development
D000890:Anti-Infective Agents; D008051:Lipid Bilayers; D009842:Oligopeptides; C402895:tritrpticin