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Interaction mode of a symmetric Trp‐rich undeca peptide PST11‐RK with lipid bilayers
Author(s) -
Yang Sung-Tae,
Shin Song Yub,
Kim Jae Il
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.12.003
Subject(s) - chemistry , peptide , lipid bilayer , biophysics , biochemistry , membrane , biology
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.