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Updated: Jul 18, 2026

Realistic Membrane Modeling Using Complex Lipid Mixtures in Simulation Studies
Published on: September 1, 2023
Interaction mode of a symmetric Trp-rich undeca peptide PST11-RK with lipid bilayers
Sung-Tae Yang1, Song Yub Shin, Jae Il Kim
1Department of Life Science, Gwangju Institute of Science and Technology, Gwangju, South Korea.
Abstract:
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.
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