Determination of Membrane Peptide Orientation by 1H-Detected 2H NMR Spectroscopy

Yamaguchi, Satoru; Hong, Mei

doi:10.1006/jmre.2002.2517

“…Solid-state NMR 31 and the proton inverse detected deuteron (PRIDE) NMR technique 36 indicate that ovispirin prefers to bind nearly parallel to the membrane-water interface (this corresponds to the final simulation conformation) and is not positioned across the bilayer (this corresponds to the starting simulation configuration). In both experiments, the peptide was reconstituted in lipid vesicles composed of (POPC: palmitoyloleoyl-phosphatidylcholine, POPG: palmitoyl-oleoyl-phosphatidylglycerol) lipids in a 3:1 ratio.…”

Section: Resultsmentioning

confidence: 99%

Molecular dynamics simulations of helical antimicrobial peptides in SDS micelles: What do point mutations achieve?

Khandelia

¹

,

Kaznessis

²

2005

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We have carried out a 40-ns all-atom molecular dynamics simulation of the helical antimicrobial peptide ovispirin-1 (OVIS) in a zwitterionic diphosphocholine (DPC) micelle. The DPC micelle serves as an economical and effective model for a cellular membrane owing to the presence of a choline headgroup, which resembles those of membrane phospholipids. OVIS, which was initially placed along a micelle diameter, diffuses out to the water-DPC interface, and the simulation stabilizes to an interface-bound steady state in 40 ns. The helical content of the peptide marginally increases in the process. The final conformation, orientation, and the structure of OVIS are in excellent agreement with the experimentally observed properties of the peptide in the presence of lipid bilayers composed of 75% zwitterionic lipids. The amphipathic peptide binds to the micelle with its hydrophobic face buried in the micellar core and the polar side chains protruding into the aqueous phase. There is overwhelming evidence that points to the significant and indispensable participation of hydrophobic residues in binding to the zwitterionic interface. The simulation starts with a conformation that is unbiased toward the final experimentally known binding state of the peptide. The ability of the model to reproduce experimental binding states despite this starting conformation is encouraging.

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“…Solid-state NMR 31 and the proton inverse detected deuteron (PRIDE) NMR technique indicate that ovispirin prefers to bind nearly parallel to the membrane−water interface (this corresponds to the final simulation conformation) and is not positioned across the bilayer (this corresponds to the starting simulation configuration). In both experiments, the peptide was reconstituted in lipid vesicles composed of (POPC: palmitoyl-oleoyl-phosphatidylcholine, POPG: palmitoyl-oleoyl-phosphatidylglycerol) lipids in a 3:1 ratio.…”

Section: Resultsmentioning

confidence: 99%

Molecular Dynamics Simulations of the Helical Antimicrobial Peptide Ovispirin-1 in a Zwitterionic Dodecylphosphocholine Micelle: Insights into Host-Cell Toxicity

Khandelia

¹

,

Kaznessis

²

2005

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We have carried out a 40-ns all-atom molecular dynamics simulation of the helical antimicrobial peptide ovispirin-1 (OVIS) in a zwitterionic diphosphocholine (DPC) micelle. The DPC micelle serves as an economical and effective model for a cellular membrane owing to the presence of a choline headgroup, which resembles those of membrane phospholipids. OVIS, which was initially placed along a micelle diameter, diffuses out to the water-DPC interface, and the simulation stabilizes to an interface-bound steady state in 40 ns. The helical content of the peptide marginally increases in the process. The final conformation, orientation, and the structure of OVIS are in excellent agreement with the experimentally observed properties of the peptide in the presence of lipid bilayers composed of 75% zwitterionic lipids. The amphipathic peptide binds to the micelle with its hydrophobic face buried in the micellar core and the polar side chains protruding into the aqueous phase. There is overwhelming evidence that points to the significant and indispensable participation of hydrophobic residues in binding to the zwitterionic interface. The simulation starts with a conformation that is unbiased toward the final experimentally known binding state of the peptide. The ability of the model to reproduce experimental binding states despite this starting conformation is encouraging.

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“…A possible strategy that also increases the weak deuterium signal up to 20-fold, is to use proton inverse detected deuterium (PRIDE) NMR. This experiment has been applied to ovispirin and gramicidin D (108). Briefly, the sequence starts with generating 1 H-2 H heteronuclear multiple quantum coherence, which then evolves under the 2 H quadrupolar interaction for a certain time, and is finally refocussed to 1 H single quantum coherence for detection.…”

Section: H Nmr On Peptidesmentioning

confidence: 99%

NMR methods for studying membrane‐active antimicrobial peptides

Strandberg

¹

,

Ulrich

²

2004

Concepts Magnetic Resonance

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NMR is a versatile tool for studying interactions between antimicrobial peptides and lipid membranes. Different approaches using both liquid state and solid state NMR are outlined here, with an emphasis on solid state NMR methods, to study the structures of antimicrobial peptides in lipid bilayers as well as the effect of these peptides on model membranes. Different NMR techniques for observing both peptides and lipids are explained, including

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Determination of Membrane Peptide Orientation by 1H-Detected 2H NMR Spectroscopy

Cited by 9 publications

References 35 publications

Molecular dynamics simulations of helical antimicrobial peptides in SDS micelles: What do point mutations achieve?

Molecular dynamics simulations of helical antimicrobial peptides in SDS micelles: What do point mutations achieve?

Molecular Dynamics Simulations of the Helical Antimicrobial Peptide Ovispirin-1 in a Zwitterionic Dodecylphosphocholine Micelle: Insights into Host-Cell Toxicity

NMR methods for studying membrane‐active antimicrobial peptides

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