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Headgroup specificity for the interaction of the antimicrobial peptide tritrpticin with phospholipid Langmuir monolayers.
Luiz C Salay, Marystela Ferreira, Osvaldo N Oliveira, Clovis R Nakaie, Shirley Schreier
Department of Biochemistry, Institute of Chemistry, University of São Paulo, São Paulo, SP, Brazil.
Colloids and surfaces. B, Biointerfaces 2012 Dec 1
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We examined the interaction of the cationic antimicrobial peptide (AMP) tritrpticin (VRRFPWWWPFLRR, TRP3) with Langmuir monolayers of zwitterionic (dipalmitoyl phosphatidylcholine, DPPC, and dipalmitoyl phosphatidylethanolamine, DPPE) and negatively charged phospholipids (dipalmitoyl phosphatidic acid, DPPA, and dipalmitoyl phosphatidylglycerol, DPPG). Both surface pressure and surface potential isotherms became more expanded upon addition of TRP3 (DPPE~DPPC<phospholipids agrees with data for vesicles and planar lipid bilayers, and with AMPs greater activity against bacterial membranes versus mammalian cell membranes. Considerable expansion of negatively charged monolayers occurred at 10 and 30 mol% TRP3, especially at low surface pressure. Moreover, a difference was observed between PA and PG, demonstrating that the interaction, besides being modulated by electrostatic interactions, displays specificity with regard to headgroup, being more pronounced in the case of PG, present in large quantities in bacterial membranes. In previous studies, it was proposed that the peptide acts by a toroidal pore-like mechanism. Considering the evidence from the literature that PG shows a propensity to form a positive curvature as do toroidal pores, the observation of TRP3's preference for the PG headgroup and the dramatic increase in area promoted by this interaction represent further support for the toroidal pore mechanism of action proposed for TRP3. Copyright © 2012 Elsevier B.V. All rights reserved.
Citation
Luiz C Salay, Marystela Ferreira, Osvaldo N Oliveira, Clovis R Nakaie, Shirley Schreier.
Headgroup specificity for the interaction of the antimicrobial peptide tritrpticin with phospholipid Langmuir monolayers.
Colloids and surfaces. B, Biointerfaces.
2012 Dec 1;100:95-102
Mesh Tags
1,2-Dipalmitoylphosphatidylcholine
Anti-Bacterial Agents
Antimicrobial Cationic Peptides
Bacteria
Cell Membrane
Eukaryotic Cells
Membranes, Artificial
Models, Molecular
Oligopeptides
Phosphatidic Acids
Phosphatidylethanolamines
Phosphatidylglycerols
Static Electricity
Surface Properties
Thermodynamics
Substances
Anti-Bacterial Agents
Antimicrobial Cationic Peptides
Membranes, Artificial
Oligopeptides
Phosphatidic Acids
Phosphatidylethanolamines
Phosphatidylglycerols
tritrpticin
dipalmitoylphosphatidic acid
1,2-Dipalmitoylphosphatidylcholine
1,2-dipalmitoyl-3-phosphatidylethanolamine
1,2-dipalmitoylphosphatidylglycerol
PMID: 22772075
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