‘Boomerang’‐like insertion of a fusogenic peptide in a lipid membrane revealed by solid‐state 19F NMR
Identifieur interne : 001B77 ( Istex/Curation ); précédent : 001B76; suivant : 001B78‘Boomerang’‐like insertion of a fusogenic peptide in a lipid membrane revealed by solid‐state 19F NMR
Auteurs : Sergii Afonin [Allemagne] ; Ulrich H. N. Dürr [Allemagne] ; Ralf W. Glaser [Allemagne] ; Anne S. Ulrich [Allemagne]Source :
- Magnetic Resonance in Chemistry [ 0749-1581 ] ; 2004-02.
English descriptors
- Teeft :
- Additional orientational constraints, Alignment, Amino acid, Amino acids, Analogue, Apposing membranes, Azimuthal, Azimuthal rotation, Bilayer, Bilayer surface, Biol, Biophys, Chem, Chemical shifts, Conformation, Considerable perturbation, Constraint, Copyright, Data analysis, Detergent micelles, Deutsche forschungsgemeinschaft, Energy barrier, Forschungszentrum karlsruhe, Free phenyl rotation, Functional state, Fusion peptide, Fusion peptides, Fusogenic, Fusogenic peptide, Germany university, Helical, Helical conformation, Helical parts, Helical structure, Helix, Isotropic chemical shift, John wiley sons, Lipid, Lipid bilayer, Local mobility, Magn, Membrane, Membrane fusion, Membrane samples, Order parameter sphg, Orientational, Orientational constraints, Other hand, Overall alignment, Peptide, Peptide alignment, Peptide analogues, Peptide backbone, Peptide rotation, Peptide segments, Peptide structure, Phenyl, Phenyl ring, Reson, Same motif, Secondary structure element, Secondary structure elements, Smol, Sphg, Structural model, Structure analysis, Structure element, Tensor, Tensor elements, Tilt angle, Torsion, Torsion angle, Tripeptide segments, Ulrich, Upper panel.
Abstract
Solid state 19F NMR revealed the conformation and alignment of the fusogenic peptide sequence B18 from the sea urchin fertilization protein bindin embedded in flat phospholipid bilayers. Single 19F labels were introduced into nine distinct positions along the wild‐type sequence by substituting each hydrophobic amino acid, one by one, with L‐4‐fluorophenylglycine. Their anisotropic chemical shifts were measured in uniaxially oriented membrane samples and used as orientational constraints to model the peptide structure in the membrane‐bound state. Previous 1H NMR studies of B18 in 30% TFE and in detergent micelles had shown that the peptide structure consists of two α‐helical segments that are connected by a flexible hinge. This helix–break–helix motif was confirmed here by the solid‐state 19F NMR data, while no other secondary structure (β‐sheet, 310‐helix) was compatible with the set of orientational constraints. For both α‐helical segments we found that the helical conformation extends all the way to the respective N‐ and C‐termini of the peptide. Analysis of the corresponding tilt and azimuthal rotation angles showed that the N‐terminal helix of B18 is immersed obliquely into the bilayer (at a tilt angle τ ≈ 54°), whereas the C‐terminus is peripherally aligned (τ ≈ 91°). The azimuthal orientation of the two segments is consistent with the amphiphilic distribution of side‐chains. The observed ‘boomerang’‐like mode of insertion into the membrane may thus explain how peptide binding leads to lipid dehydration and acyl chain perturbation as a prerequisite for bilayer fusion to occur. Copyright © 2004 John Wiley & Sons, Ltd.
Url:
DOI: 10.1002/mrc.1340
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Glaser</name><affiliation wicri:level="1"><mods:affiliation>University of Jena, Institute of Biochemistry & Biophysics, Hans‐Knöll‐Strasse 2, 07745 Jena, Germany</mods:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>University of Jena, Institute of Biochemistry & Biophysics, Hans‐Knöll‐Strasse 2, 07745 Jena</wicri:regionArea></affiliation></author><author><name sortKey="Ulrich, Anne S" sort="Ulrich, Anne S" uniqKey="Ulrich A" first="Anne S." last="Ulrich">Anne S. Ulrich</name><affiliation wicri:level="1"><mods:affiliation>Forschungszentrum Karlsruhe, IFIA, POB 3640, 76021 Karlsruhe, Germany</mods:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Forschungszentrum Karlsruhe, IFIA, POB 3640, 76021 Karlsruhe</wicri:regionArea></affiliation><affiliation wicri:level="1"><mods:affiliation>University of Karlsruhe, Institute of Organic Chemistry, Fritz‐Haber‐Weg 6, 76131 Karlsruhe, Germany</mods:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>University of Karlsruhe, Institute of Organic Chemistry, Fritz‐Haber‐Weg 6, 76131 Karlsruhe</wicri:regionArea></affiliation><affiliation wicri:level="1"><mods:affiliation>E-mail: anne.ulrich@ifia.fzk.de</mods:affiliation><country wicri:rule="url">Allemagne</country></affiliation><affiliation wicri:level="1"><mods:affiliation>Correspondence address: Forschungszentrum Karlsruhe, POB 3640, 76021 Karlsruhe, Germany.===</mods:affiliation><country xml:lang="fr" wicri:curation="lc">Allemagne</country><wicri:regionArea>Correspondence address: Forschungszentrum Karlsruhe, POB 3640, 76021 Karlsruhe</wicri:regionArea></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Magnetic Resonance in Chemistry</title><title level="j" type="sub">Solid‐state NMR on biological systems</title><title level="j" type="alt">MAGNETIC RESONANCE IN CHEMISTRY</title><idno type="ISSN">0749-1581</idno><idno type="eISSN">1097-458X</idno><imprint><biblScope unit="vol">42</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="195">195</biblScope><biblScope unit="page" to="203">203</biblScope><biblScope unit="page-count">9</biblScope><publisher>John Wiley & Sons, Ltd.</publisher><pubPlace>Chichester, UK</pubPlace><date type="published" when="2004-02">2004-02</date></imprint><idno type="ISSN">0749-1581</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0749-1581</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Additional orientational constraints</term><term>Alignment</term><term>Amino acid</term><term>Amino acids</term><term>Analogue</term><term>Apposing membranes</term><term>Azimuthal</term><term>Azimuthal rotation</term><term>Bilayer</term><term>Bilayer surface</term><term>Biol</term><term>Biophys</term><term>Chem</term><term>Chemical shifts</term><term>Conformation</term><term>Considerable perturbation</term><term>Constraint</term><term>Copyright</term><term>Data analysis</term><term>Detergent micelles</term><term>Deutsche forschungsgemeinschaft</term><term>Energy barrier</term><term>Forschungszentrum karlsruhe</term><term>Free phenyl rotation</term><term>Functional state</term><term>Fusion peptide</term><term>Fusion peptides</term><term>Fusogenic</term><term>Fusogenic peptide</term><term>Germany university</term><term>Helical</term><term>Helical conformation</term><term>Helical parts</term><term>Helical structure</term><term>Helix</term><term>Isotropic chemical shift</term><term>John wiley sons</term><term>Lipid</term><term>Lipid bilayer</term><term>Local mobility</term><term>Magn</term><term>Membrane</term><term>Membrane fusion</term><term>Membrane samples</term><term>Order parameter sphg</term><term>Orientational</term><term>Orientational constraints</term><term>Other hand</term><term>Overall alignment</term><term>Peptide</term><term>Peptide alignment</term><term>Peptide analogues</term><term>Peptide backbone</term><term>Peptide rotation</term><term>Peptide segments</term><term>Peptide structure</term><term>Phenyl</term><term>Phenyl ring</term><term>Reson</term><term>Same motif</term><term>Secondary structure element</term><term>Secondary structure elements</term><term>Smol</term><term>Sphg</term><term>Structural model</term><term>Structure analysis</term><term>Structure element</term><term>Tensor</term><term>Tensor elements</term><term>Tilt angle</term><term>Torsion</term><term>Torsion angle</term><term>Tripeptide segments</term><term>Ulrich</term><term>Upper panel</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Solid state 19F NMR revealed the conformation and alignment of the fusogenic peptide sequence B18 from the sea urchin fertilization protein bindin embedded in flat phospholipid bilayers. Single 19F labels were introduced into nine distinct positions along the wild‐type sequence by substituting each hydrophobic amino acid, one by one, with L‐4‐fluorophenylglycine. Their anisotropic chemical shifts were measured in uniaxially oriented membrane samples and used as orientational constraints to model the peptide structure in the membrane‐bound state. Previous 1H NMR studies of B18 in 30% TFE and in detergent micelles had shown that the peptide structure consists of two α‐helical segments that are connected by a flexible hinge. This helix–break–helix motif was confirmed here by the solid‐state 19F NMR data, while no other secondary structure (β‐sheet, 310‐helix) was compatible with the set of orientational constraints. For both α‐helical segments we found that the helical conformation extends all the way to the respective N‐ and C‐termini of the peptide. Analysis of the corresponding tilt and azimuthal rotation angles showed that the N‐terminal helix of B18 is immersed obliquely into the bilayer (at a tilt angle τ ≈ 54°), whereas the C‐terminus is peripherally aligned (τ ≈ 91°). The azimuthal orientation of the two segments is consistent with the amphiphilic distribution of side‐chains. The observed ‘boomerang’‐like mode of insertion into the membrane may thus explain how peptide binding leads to lipid dehydration and acyl chain perturbation as a prerequisite for bilayer fusion to occur. Copyright © 2004 John Wiley & Sons, Ltd.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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