Conformational study of new amphipathic α‐helical peptide models of apoA‐I as potential atheroprotective agents
Identifieur interne : 000A13 ( Istex/Corpus ); précédent : 000A12; suivant : 000A14Conformational study of new amphipathic α‐helical peptide models of apoA‐I as potential atheroprotective agents
Auteurs : Chrystel Beaufils ; Charalampos Alexopoulos ; Maria P. Petraki ; Alexandros D. Tselepis ; Nicolas Coudevylle ; Maria Sakarellos-Daitsiotis ; Constantinos Sakarellos ; Manh Thong CungSource :
- Peptide Science [ 0006-3525 ] ; 2007.
English descriptors
- KwdEn :
- Amide, Amino, Amino acids, Amino residues, Amphipathic, Amphipathic character, Amphipathic helices, Amphipathic helix, Angle values, Antioxidant, Antioxidant activity, Antioxidant effect, Antioxidant properties, Aqueous solution, Atheroprotective, Average structure, Backbone ribbon, Beckman ultracentrifuge, Biochim biophys acta, Biol, Biol chem, Biopolymers, Blue line, Brouillette, Chem, Conformation, Conformational study, Dialysis tubes, Diene formation, Dienes, Different line thicknesses, Different phospholipids, Dihedral angle values, Edmundson helical wheel projection, Ethyl alcohol, Exchange kinetics, Gentamicine sulphate, Green line, Helical, Helical conformation, Helical peptide models, Helix, Helix fragments, Helix structure, Human plasma, Hydrogen bonds, Hydrophilic face, Hydrophobic, Hydrophobic face, Hydrophobic residues, Local conformation, Maximal rate, Mixtures molar ratio, Molar, Molar ratio, Molecular dynamics simulation, Molecular mass cutoff, Molmol software, Noesy experiments, Nonpolar face, Numerous medium, Oxidant scavenger, Palmitoyl groups, Peptide, Peptide backbone, Peptide concentration, Peptide model, Peptide models, Peptide protein, Peptide science, Peptide synthesis, Potential atheroprotective agents, Proc natl acad, Purple line, Residue, Scavenger, Secondary structure, Sequential centrifugation, Serine residues, Side view, Simulation, Solid state, Structural motif, Threshold concentration, Torsion angle model, Total amount, Uorescence spectroscopy, Wiley periodicals.
- Teeft :
- Amide, Amino, Amino acids, Amino residues, Amphipathic, Amphipathic character, Amphipathic helices, Amphipathic helix, Angle values, Antioxidant, Antioxidant activity, Antioxidant effect, Antioxidant properties, Aqueous solution, Atheroprotective, Average structure, Backbone ribbon, Beckman ultracentrifuge, Biochim biophys acta, Biol, Biol chem, Biopolymers, Blue line, Brouillette, Chem, Conformation, Conformational study, Dialysis tubes, Diene formation, Dienes, Different line thicknesses, Different phospholipids, Dihedral angle values, Edmundson helical wheel projection, Ethyl alcohol, Exchange kinetics, Gentamicine sulphate, Green line, Helical, Helical conformation, Helical peptide models, Helix, Helix fragments, Helix structure, Human plasma, Hydrogen bonds, Hydrophilic face, Hydrophobic, Hydrophobic face, Hydrophobic residues, Local conformation, Maximal rate, Mixtures molar ratio, Molar, Molar ratio, Molecular dynamics simulation, Molecular mass cutoff, Molmol software, Noesy experiments, Nonpolar face, Numerous medium, Oxidant scavenger, Palmitoyl groups, Peptide, Peptide backbone, Peptide concentration, Peptide model, Peptide models, Peptide protein, Peptide science, Peptide synthesis, Potential atheroprotective agents, Proc natl acad, Purple line, Residue, Scavenger, Secondary structure, Sequential centrifugation, Serine residues, Side view, Simulation, Solid state, Structural motif, Threshold concentration, Torsion angle model, Total amount, Uorescence spectroscopy, Wiley periodicals.
Abstract
Aiming at contributing to the development of potential atheroprotective agents, we report on the concept and design of two peptide models, which mimic the amphipathic helices of apoA‐I and incorporate Met into their sequences to validate its role as oxidant scavenger: Ac‐ESK(Palm)KELSKSW10SEM13LKEK(Palm)SKS‐NH2 (model 1 [W10, M13]) and Ac‐ESK(Palm)KELSKSM10SEW13LKEK(Palm)SKS‐NH2 (model 2 [M10, W13]). Hydrophobic residues of both models cover about the half of the surface, while the positively and negatively charged residues constitute two separate clusters on the hydrophilic face. Palmitoyl groups were introduced into the Lys‐NϵH2 groups at positions 3 and 17 to contribute to the amphipathic character of the peptides and stabilize the nonpolar face of the helix. Conformational study by the combined application of 2D‐NMR and molecular dynamics simulations, CD, FTIR, and fluorescence spectroscopy revealed that model 1 adopts helical conformation and Met is well exposed to the microenvironment. Model 2 that derives from model 1 by exchanging W10 (model 1) with M10 and M13 (model 1) with W13 also displays helical characteristics, while Met is rather shielded. Oxidation experiments indicated that model 1 exhibits a 2‐fold more potent antioxidant activity towards LDL oxidation, compared to model 2, confirming the role of Met, when is devoid of steric hindrances, as oxidant scavenger for the protection of LDL. © 2006 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 88: 362–372, 2007. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com
Url:
DOI: 10.1002/bip.20651
Links to Exploration step
ISTEX:E2DF581AC3537D55048491AF88943DF1F02B76C8Le document en format XML
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Petraki</name><affiliation><mods:affiliation>Department of Chemistry, University of Ioannina, Box 1186, 451 10 Ioannina, Greece</mods:affiliation></affiliation></author><author><name sortKey="Tselepis, Alexandros D" sort="Tselepis, Alexandros D" uniqKey="Tselepis A" first="Alexandros D." last="Tselepis">Alexandros D. Tselepis</name><affiliation><mods:affiliation>Department of Chemistry, University of Ioannina, Box 1186, 451 10 Ioannina, Greece</mods:affiliation></affiliation></author><author><name sortKey="Coudevylle, Nicolas" sort="Coudevylle, Nicolas" uniqKey="Coudevylle N" first="Nicolas" last="Coudevylle">Nicolas Coudevylle</name><affiliation><mods:affiliation>Laboratoire de Chimie‐Physique Macromoléculaire, UMR 7568 CNRS‐INPL, ENSIC, 1 rue Grandville, B.P. 20451, 54001 Nancy Cedex, France</mods:affiliation></affiliation></author><author><name sortKey="Sakarellos Aitsiotis, Maria" sort="Sakarellos Aitsiotis, Maria" uniqKey="Sakarellos Aitsiotis M" first="Maria" last="Sakarellos-Daitsiotis">Maria Sakarellos-Daitsiotis</name><affiliation><mods:affiliation>Department of Chemistry, University of Ioannina, Box 1186, 451 10 Ioannina, Greece</mods:affiliation></affiliation><affiliation><mods:affiliation>E-mail: msakarel@uoi.gr</mods:affiliation></affiliation><affiliation><mods:affiliation>Maria Sakarellos‐Daitsiotis, Department of Chemistry, University of Ioannina, Box 1186, 451 10 Ioannina, GreeceManh Thong Cung, Laboratoire de Chimie‐Physique Macromoléculaire, UMR 7568 CNRS‐INPL, ENSIC, 1 rue Grandville, B.P. 20451, 54001 Nancy Cedex, France</mods:affiliation></affiliation></author><author><name sortKey="Sakarellos, Constantinos" sort="Sakarellos, Constantinos" uniqKey="Sakarellos C" first="Constantinos" last="Sakarellos">Constantinos Sakarellos</name><affiliation><mods:affiliation>Department of Chemistry, University of Ioannina, Box 1186, 451 10 Ioannina, Greece</mods:affiliation></affiliation></author><author><name sortKey="Cung, Manh Thong" sort="Cung, Manh Thong" uniqKey="Cung M" first="Manh Thong" last="Cung">Manh Thong Cung</name><affiliation><mods:affiliation>Laboratoire de Chimie‐Physique Macromoléculaire, UMR 7568 CNRS‐INPL, ENSIC, 1 rue Grandville, B.P. 20451, 54001 Nancy Cedex, France</mods:affiliation></affiliation><affiliation><mods:affiliation>E-mail: manh‐thong.cung@ensic.inpl‐nancy.fr</mods:affiliation></affiliation><affiliation><mods:affiliation>Maria Sakarellos‐Daitsiotis, Department of Chemistry, University of Ioannina, Box 1186, 451 10 Ioannina, GreeceManh Thong Cung, Laboratoire de Chimie‐Physique Macromoléculaire, UMR 7568 CNRS‐INPL, ENSIC, 1 rue Grandville, B.P. 20451, 54001 Nancy Cedex, France</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Peptide Science</title><title level="j" type="alt">PEPTIDE SCIENCE</title><idno type="ISSN">0006-3525</idno><idno type="eISSN">1097-0282</idno><imprint><biblScope unit="vol">88</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="362">362</biblScope><biblScope unit="page" to="372">372</biblScope><biblScope unit="page-count">11</biblScope><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><date type="published" when="2007">2007</date></imprint><idno type="ISSN">0006-3525</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0006-3525</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amide</term><term>Amino</term><term>Amino acids</term><term>Amino residues</term><term>Amphipathic</term><term>Amphipathic character</term><term>Amphipathic helices</term><term>Amphipathic helix</term><term>Angle values</term><term>Antioxidant</term><term>Antioxidant activity</term><term>Antioxidant effect</term><term>Antioxidant properties</term><term>Aqueous solution</term><term>Atheroprotective</term><term>Average structure</term><term>Backbone ribbon</term><term>Beckman ultracentrifuge</term><term>Biochim biophys acta</term><term>Biol</term><term>Biol chem</term><term>Biopolymers</term><term>Blue line</term><term>Brouillette</term><term>Chem</term><term>Conformation</term><term>Conformational study</term><term>Dialysis tubes</term><term>Diene formation</term><term>Dienes</term><term>Different line thicknesses</term><term>Different phospholipids</term><term>Dihedral angle values</term><term>Edmundson helical wheel projection</term><term>Ethyl alcohol</term><term>Exchange kinetics</term><term>Gentamicine sulphate</term><term>Green line</term><term>Helical</term><term>Helical conformation</term><term>Helical peptide models</term><term>Helix</term><term>Helix fragments</term><term>Helix structure</term><term>Human plasma</term><term>Hydrogen bonds</term><term>Hydrophilic face</term><term>Hydrophobic</term><term>Hydrophobic face</term><term>Hydrophobic residues</term><term>Local conformation</term><term>Maximal rate</term><term>Mixtures molar ratio</term><term>Molar</term><term>Molar ratio</term><term>Molecular dynamics simulation</term><term>Molecular mass cutoff</term><term>Molmol software</term><term>Noesy experiments</term><term>Nonpolar face</term><term>Numerous medium</term><term>Oxidant scavenger</term><term>Palmitoyl groups</term><term>Peptide</term><term>Peptide backbone</term><term>Peptide concentration</term><term>Peptide model</term><term>Peptide models</term><term>Peptide protein</term><term>Peptide science</term><term>Peptide synthesis</term><term>Potential atheroprotective agents</term><term>Proc natl acad</term><term>Purple line</term><term>Residue</term><term>Scavenger</term><term>Secondary structure</term><term>Sequential centrifugation</term><term>Serine residues</term><term>Side view</term><term>Simulation</term><term>Solid state</term><term>Structural motif</term><term>Threshold concentration</term><term>Torsion angle model</term><term>Total amount</term><term>Uorescence spectroscopy</term><term>Wiley periodicals</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Amide</term><term>Amino</term><term>Amino acids</term><term>Amino residues</term><term>Amphipathic</term><term>Amphipathic character</term><term>Amphipathic helices</term><term>Amphipathic helix</term><term>Angle values</term><term>Antioxidant</term><term>Antioxidant activity</term><term>Antioxidant effect</term><term>Antioxidant properties</term><term>Aqueous solution</term><term>Atheroprotective</term><term>Average structure</term><term>Backbone ribbon</term><term>Beckman ultracentrifuge</term><term>Biochim biophys acta</term><term>Biol</term><term>Biol chem</term><term>Biopolymers</term><term>Blue line</term><term>Brouillette</term><term>Chem</term><term>Conformation</term><term>Conformational study</term><term>Dialysis tubes</term><term>Diene formation</term><term>Dienes</term><term>Different line thicknesses</term><term>Different phospholipids</term><term>Dihedral angle values</term><term>Edmundson helical wheel projection</term><term>Ethyl alcohol</term><term>Exchange kinetics</term><term>Gentamicine sulphate</term><term>Green line</term><term>Helical</term><term>Helical conformation</term><term>Helical peptide models</term><term>Helix</term><term>Helix fragments</term><term>Helix structure</term><term>Human plasma</term><term>Hydrogen bonds</term><term>Hydrophilic face</term><term>Hydrophobic</term><term>Hydrophobic face</term><term>Hydrophobic residues</term><term>Local conformation</term><term>Maximal rate</term><term>Mixtures molar ratio</term><term>Molar</term><term>Molar ratio</term><term>Molecular dynamics simulation</term><term>Molecular mass cutoff</term><term>Molmol software</term><term>Noesy experiments</term><term>Nonpolar face</term><term>Numerous medium</term><term>Oxidant scavenger</term><term>Palmitoyl groups</term><term>Peptide</term><term>Peptide backbone</term><term>Peptide concentration</term><term>Peptide model</term><term>Peptide models</term><term>Peptide protein</term><term>Peptide science</term><term>Peptide synthesis</term><term>Potential atheroprotective agents</term><term>Proc natl acad</term><term>Purple line</term><term>Residue</term><term>Scavenger</term><term>Secondary structure</term><term>Sequential centrifugation</term><term>Serine residues</term><term>Side view</term><term>Simulation</term><term>Solid state</term><term>Structural motif</term><term>Threshold concentration</term><term>Torsion angle model</term><term>Total amount</term><term>Uorescence spectroscopy</term><term>Wiley periodicals</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Aiming at contributing to the development of potential atheroprotective agents, we report on the concept and design of two peptide models, which mimic the amphipathic helices of apoA‐I and incorporate Met into their sequences to validate its role as oxidant scavenger: Ac‐ESK(Palm)KELSKSW10SEM13LKEK(Palm)SKS‐NH2 (model 1 [W10, M13]) and Ac‐ESK(Palm)KELSKSM10SEW13LKEK(Palm)SKS‐NH2 (model 2 [M10, W13]). Hydrophobic residues of both models cover about the half of the surface, while the positively and negatively charged residues constitute two separate clusters on the hydrophilic face. Palmitoyl groups were introduced into the Lys‐NϵH2 groups at positions 3 and 17 to contribute to the amphipathic character of the peptides and stabilize the nonpolar face of the helix. Conformational study by the combined application of 2D‐NMR and molecular dynamics simulations, CD, FTIR, and fluorescence spectroscopy revealed that model 1 adopts helical conformation and Met is well exposed to the microenvironment. Model 2 that derives from model 1 by exchanging W10 (model 1) with M10 and M13 (model 1) with W13 also displays helical characteristics, while Met is rather shielded. Oxidation experiments indicated that model 1 exhibits a 2‐fold more potent antioxidant activity towards LDL oxidation, compared to model 2, confirming the role of Met, when is devoid of steric hindrances, as oxidant scavenger for the protection of LDL. © 2006 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 88: 362–372, 2007. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com</div></front></TEI><istex><corpusName>wiley</corpusName><keywords><teeft><json:string>peptide</json:string><json:string>peptide model</json:string><json:string>helix</json:string><json:string>helical</json:string><json:string>amphipathic</json:string><json:string>peptide models</json:string><json:string>biopolymers</json:string><json:string>antioxidant</json:string><json:string>peptide science</json:string><json:string>biol</json:string><json:string>chem</json:string><json:string>helical peptide models</json:string><json:string>dienes</json:string><json:string>brouillette</json:string><json:string>atheroprotective</json:string><json:string>total amount</json:string><json:string>oxidant scavenger</json:string><json:string>hydrophobic residues</json:string><json:string>amino</json:string><json:string>nonpolar face</json:string><json:string>helix structure</json:string><json:string>hydrogen bonds</json:string><json:string>antioxidant activity</json:string><json:string>amide</json:string><json:string>scavenger</json:string><json:string>molar</json:string><json:string>helical conformation</json:string><json:string>biol chem</json:string><json:string>conformational study</json:string><json:string>peptide concentration</json:string><json:string>mixtures molar ratio</json:string><json:string>hydrophilic face</json:string><json:string>palmitoyl groups</json:string><json:string>aqueous solution</json:string><json:string>amino residues</json:string><json:string>amphipathic character</json:string><json:string>dihedral angle values</json:string><json:string>amphipathic helices</json:string><json:string>side view</json:string><json:string>biochim biophys acta</json:string><json:string>residue</json:string><json:string>conformation</json:string><json:string>simulation</json:string><json:string>hydrophobic</json:string><json:string>antioxidant properties</json:string><json:string>ethyl alcohol</json:string><json:string>solid state</json:string><json:string>human plasma</json:string><json:string>gentamicine sulphate</json:string><json:string>sequential centrifugation</json:string><json:string>beckman ultracentrifuge</json:string><json:string>maximal rate</json:string><json:string>diene formation</json:string><json:string>local conformation</json:string><json:string>amino acids</json:string><json:string>threshold concentration</json:string><json:string>hydrophobic face</json:string><json:string>serine residues</json:string><json:string>dialysis tubes</json:string><json:string>numerous medium</json:string><json:string>different line thicknesses</json:string><json:string>helix fragments</json:string><json:string>molecular mass cutoff</json:string><json:string>peptide backbone</json:string><json:string>proc natl acad</json:string><json:string>molmol software</json:string><json:string>uorescence spectroscopy</json:string><json:string>molecular dynamics simulation</json:string><json:string>torsion angle model</json:string><json:string>structural motif</json:string><json:string>angle values</json:string><json:string>molar ratio</json:string><json:string>average structure</json:string><json:string>edmundson helical wheel projection</json:string><json:string>backbone ribbon</json:string><json:string>blue line</json:string><json:string>green line</json:string><json:string>purple line</json:string><json:string>exchange kinetics</json:string><json:string>antioxidant effect</json:string><json:string>wiley periodicals</json:string><json:string>secondary structure</json:string><json:string>noesy experiments</json:string><json:string>amphipathic helix</json:string><json:string>potential atheroprotective agents</json:string><json:string>peptide synthesis</json:string><json:string>peptide protein</json:string><json:string>different phospholipids</json:string></teeft></keywords><author><json:item><name>Chrystel Beaufils</name><affiliations><json:string>Laboratoire de Chimie‐Physique Macromoléculaire, UMR 7568 CNRS‐INPL, ENSIC, 1 rue Grandville, B.P. 20451, 54001 Nancy Cedex, France</json:string></affiliations></json:item><json:item><name>Charalampos Alexopoulos</name><affiliations><json:string>Department of Chemistry, University of Ioannina, Box 1186, 451 10 Ioannina, Greece</json:string></affiliations></json:item><json:item><name>Maria P. Petraki</name><affiliations><json:string>Department of Chemistry, University of Ioannina, Box 1186, 451 10 Ioannina, Greece</json:string></affiliations></json:item><json:item><name>Alexandros D. Tselepis</name><affiliations><json:string>Department of Chemistry, University of Ioannina, Box 1186, 451 10 Ioannina, Greece</json:string></affiliations></json:item><json:item><name>Nicolas Coudevylle</name><affiliations><json:string>Laboratoire de Chimie‐Physique Macromoléculaire, UMR 7568 CNRS‐INPL, ENSIC, 1 rue Grandville, B.P. 20451, 54001 Nancy Cedex, France</json:string></affiliations></json:item><json:item><name>Maria Sakarellos‐Daitsiotis</name><affiliations><json:string>Department of Chemistry, University of Ioannina, Box 1186, 451 10 Ioannina, Greece</json:string><json:string>Maria Sakarellos‐Daitsiotis, Department of Chemistry, University of Ioannina, Box 1186, 451 10 Ioannina, GreeceManh Thong Cung, Laboratoire de Chimie‐Physique Macromoléculaire, UMR 7568 CNRS‐INPL, ENSIC, 1 rue Grandville, B.P. 20451, 54001 Nancy Cedex, France</json:string></affiliations></json:item><json:item><name>Constantinos Sakarellos</name><affiliations><json:string>Department of Chemistry, University of Ioannina, Box 1186, 451 10 Ioannina, Greece</json:string></affiliations></json:item><json:item><name>Manh Thong Cung</name><affiliations><json:string>Laboratoire de Chimie‐Physique Macromoléculaire, UMR 7568 CNRS‐INPL, ENSIC, 1 rue Grandville, B.P. 20451, 54001 Nancy Cedex, France</json:string><json:string>Maria Sakarellos‐Daitsiotis, Department of Chemistry, University of Ioannina, Box 1186, 451 10 Ioannina, GreeceManh Thong Cung, Laboratoire de Chimie‐Physique Macromoléculaire, UMR 7568 CNRS‐INPL, ENSIC, 1 rue Grandville, B.P. 20451, 54001 Nancy Cedex, France</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>apolipoprotein A‐I</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>amphipathic α‐helix</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>atheroprotective peptide models</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>HDL</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>LDL</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>2D‐NMR</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>NOESY</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>molecular modeling</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>CD</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>fluorescence</value></json:item></subject><articleId><json:string>BIP20651</json:string></articleId><language><json:string>eng</json:string></language><originalGenre><json:string>article</json:string></originalGenre><abstract>Aiming at contributing to the development of potential atheroprotective agents, we report on the concept and design of two peptide models, which mimic the amphipathic helices of apoA‐I and incorporate Met into their sequences to validate its role as oxidant scavenger: Ac‐ESK(Palm)KELSKSW10SEM13LKEK(Palm)SKS‐NH2 (model 1 [W10, M13]) and Ac‐ESK(Palm)KELSKSM10SEW13LKEK(Palm)SKS‐NH2 (model 2 [M10, W13]). Hydrophobic residues of both models cover about the half of the surface, while the positively and negatively charged residues constitute two separate clusters on the hydrophilic face. Palmitoyl groups were introduced into the Lys‐NϵH2 groups at positions 3 and 17 to contribute to the amphipathic character of the peptides and stabilize the nonpolar face of the helix. Conformational study by the combined application of 2D‐NMR and molecular dynamics simulations, CD, FTIR, and fluorescence spectroscopy revealed that model 1 adopts helical conformation and Met is well exposed to the microenvironment. Model 2 that derives from model 1 by exchanging W10 (model 1) with M10 and M13 (model 1) with W13 also displays helical characteristics, while Met is rather shielded. Oxidation experiments indicated that model 1 exhibits a 2‐fold more potent antioxidant activity towards LDL oxidation, compared to model 2, confirming the role of Met, when is devoid of steric hindrances, as oxidant scavenger for the protection of LDL. © 2006 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 88: 362–372, 2007. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. 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ApoA‐I</title><author xml:id="author-0000"><persName><forename type="first">Chrystel</forename><surname>Beaufils</surname></persName><affiliation>Laboratoire de Chimie‐Physique Macromoléculaire, UMR 7568 CNRS‐INPL, ENSIC, 1 rue Grandville, B.P. 20451, 54001 Nancy Cedex, France<address><country key="FR"></country></address></affiliation></author><author xml:id="author-0001"><persName><forename type="first">Charalampos</forename><surname>Alexopoulos</surname></persName><affiliation>Department of Chemistry, University of Ioannina, Box 1186, 451 10 Ioannina, Greece<address><country key="GR"></country></address></affiliation></author><author xml:id="author-0002"><persName><forename type="first">Maria P.</forename><surname>Petraki</surname></persName><affiliation>Department of Chemistry, University of Ioannina, Box 1186, 451 10 Ioannina, Greece<address><country key="GR"></country></address></affiliation></author><author xml:id="author-0003"><persName><forename type="first">Alexandros D.</forename><surname>Tselepis</surname></persName><affiliation>Department of Chemistry, University of Ioannina, Box 1186, 451 10 Ioannina, Greece<address><country key="GR"></country></address></affiliation></author><author xml:id="author-0004"><persName><forename type="first">Nicolas</forename><surname>Coudevylle</surname></persName><affiliation>Laboratoire de Chimie‐Physique Macromoléculaire, UMR 7568 CNRS‐INPL, ENSIC, 1 rue Grandville, B.P. 20451, 54001 Nancy Cedex, France<address><country key="FR"></country></address></affiliation></author><author xml:id="author-0005" role="corresp"><persName><forename type="first">Maria</forename><surname>Sakarellos‐Daitsiotis</surname></persName><email>msakarel@uoi.gr</email><affiliation>Department of Chemistry, University of Ioannina, Box 1186, 451 10 Ioannina, Greece<address><country key="GR"></country></address></affiliation><affiliation>Maria Sakarellos‐Daitsiotis, Department of Chemistry, University of Ioannina, Box 1186, 451 10 Ioannina, Greece Manh Thong Cung, Laboratoire de Chimie‐Physique Macromoléculaire, UMR 7568 CNRS‐INPL, ENSIC, 1 rue Grandville, B.P. 20451, 54001 Nancy Cedex, France</affiliation></author><author xml:id="author-0006"><persName><forename type="first">Constantinos</forename><surname>Sakarellos</surname></persName><affiliation>Department of Chemistry, University of Ioannina, Box 1186, 451 10 Ioannina, Greece<address><country key="GR"></country></address></affiliation></author><author xml:id="author-0007" role="corresp"><persName><forename type="first">Manh Thong</forename><surname>Cung</surname></persName><email>manh‐thong.cung@ensic.inpl‐nancy.fr</email><affiliation>Laboratoire de Chimie‐Physique Macromoléculaire, UMR 7568 CNRS‐INPL, ENSIC, 1 rue Grandville, B.P. 20451, 54001 Nancy Cedex, France<address><country key="FR"></country></address></affiliation><affiliation>Maria Sakarellos‐Daitsiotis, Department of Chemistry, University of Ioannina, Box 1186, 451 10 Ioannina, Greece Manh Thong Cung, 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Hydrophobic residues of both models cover about the half of the surface, while the positively and negatively charged residues constitute two separate clusters on the hydrophilic face. Palmitoyl groups were introduced into the Lys‐N<hi rend="superscript">ϵ</hi>H<hi rend="subscript">2</hi> groups at positions 3 and 17 to contribute to the amphipathic character of the peptides and stabilize the nonpolar face of the helix. Conformational study by the combined application of 2D‐NMR and molecular dynamics simulations, CD, FTIR, and fluorescence spectroscopy revealed that model 1 adopts helical conformation and Met is well exposed to the microenvironment. Model 2 that derives from model 1 by exchanging W<hi rend="superscript">10</hi> (model 1) with M<hi rend="superscript">10</hi> and M<hi rend="superscript">13</hi> (model 1) with W<hi rend="superscript">13</hi> also displays helical characteristics, while Met is rather shielded. Oxidation experiments indicated that model 1 exhibits a 2‐fold more potent antioxidant activity towards LDL oxidation, compared to model 2, confirming the role of Met, when is devoid of steric hindrances, as oxidant scavenger for the protection of LDL. © 2006 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 88: 362–372, 2007.</p><p>This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. 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ApoA‐I</title></titleGroup><creators><creator xml:id="au1" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Chrystel</givenNames><familyName>Beaufils</familyName></personName></creator><creator xml:id="au2" creatorRole="author" affiliationRef="#af2"><personName><givenNames>Charalampos</givenNames><familyName>Alexopoulos</familyName></personName></creator><creator xml:id="au3" creatorRole="author" affiliationRef="#af2"><personName><givenNames>Maria P.</givenNames><familyName>Petraki</familyName></personName></creator><creator xml:id="au4" creatorRole="author" affiliationRef="#af2"><personName><givenNames>Alexandros D.</givenNames><familyName>Tselepis</familyName></personName></creator><creator xml:id="au5" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Nicolas</givenNames><familyName>Coudevylle</familyName></personName></creator><creator xml:id="au6" creatorRole="author" affiliationRef="#af2" corresponding="yes"><personName><givenNames>Maria</givenNames><familyName>Sakarellos‐Daitsiotis</familyName></personName><contactDetails><email>msakarel@uoi.gr</email></contactDetails></creator><creator xml:id="au7" creatorRole="author" affiliationRef="#af2"><personName><givenNames>Constantinos</givenNames><familyName>Sakarellos</familyName></personName></creator><creator xml:id="au8" creatorRole="author" affiliationRef="#af1" corresponding="yes"><personName><givenNames>Manh Thong</givenNames><familyName>Cung</familyName></personName><contactDetails><email normalForm="manh-thong.cung@ensic.inpl-nancy.fr">manh‐thong.cung@ensic.inpl‐nancy.fr</email></contactDetails></creator></creators><affiliationGroup><affiliation xml:id="af1" countryCode="FR" type="organization"><unparsedAffiliation>Laboratoire de Chimie‐Physique Macromoléculaire, UMR 7568 CNRS‐INPL, ENSIC, 1 rue Grandville, B.P. 20451, 54001 Nancy Cedex, France</unparsedAffiliation></affiliation><affiliation xml:id="af2" countryCode="GR" type="organization"><unparsedAffiliation>Department of Chemistry, University of Ioannina, Box 1186, 451 10 Ioannina, Greece</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en" type="author"><keyword xml:id="kwd1">apolipoprotein A‐I</keyword><keyword xml:id="kwd2">amphipathic α‐helix</keyword><keyword xml:id="kwd3">atheroprotective peptide models</keyword><keyword xml:id="kwd4">HDL</keyword><keyword xml:id="kwd5">LDL</keyword><keyword xml:id="kwd6">2D‐NMR</keyword><keyword xml:id="kwd7">NOESY</keyword><keyword xml:id="kwd8">molecular modeling</keyword><keyword xml:id="kwd9">CD</keyword><keyword xml:id="kwd10">fluorescence</keyword></keywordGroup><fundingInfo><fundingAgency>Centre National de la Recherche Scientifique</fundingAgency></fundingInfo><fundingInfo><fundingAgency>EPEAEK (Ministry of Education, Greece)</fundingAgency></fundingInfo><abstractGroup><abstract type="main" xml:lang="en"><title type="main">Abstract</title><p>Aiming at contributing to the development of potential atheroprotective agents, we report on the concept and design of two peptide models, which mimic the amphipathic helices of apoA‐I and incorporate Met into their sequences to validate its role as oxidant scavenger: Ac‐ESK(Palm)KELSKSW<sup>10</sup>SEM<sup>13</sup>LKEK(Palm)SKS‐NH<sub>2</sub> (model 1 [W<sup>10</sup>, M<sup>13</sup>]) and Ac‐ESK(Palm)KELSKSM<sup>10</sup>SEW<sup>13</sup>LKEK(Palm)SKS‐NH<sub>2</sub> (model 2 [M<sup>10</sup>, W<sup>13</sup>]). Hydrophobic residues of both models cover about the half of the surface, while the positively and negatively charged residues constitute two separate clusters on the hydrophilic face. Palmitoyl groups were introduced into the Lys‐N<sup>ϵ</sup>H<sub>2</sub> groups at positions 3 and 17 to contribute to the amphipathic character of the peptides and stabilize the nonpolar face of the helix. Conformational study by the combined application of 2D‐NMR and molecular dynamics simulations, CD, FTIR, and fluorescence spectroscopy revealed that model 1 adopts helical conformation and Met is well exposed to the microenvironment. Model 2 that derives from model 1 by exchanging W<sup>10</sup> (model 1) with M<sup>10</sup> and M<sup>13</sup> (model 1) with W<sup>13</sup> also displays helical characteristics, while Met is rather shielded. Oxidation experiments indicated that model 1 exhibits a 2‐fold more potent antioxidant activity towards LDL oxidation, compared to model 2, confirming the role of Met, when is devoid of steric hindrances, as oxidant scavenger for the protection of LDL. © 2006 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 88: 362–372, 2007.</p><p>This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Conformational study of new amphipathic α‐helical peptide models of apoA‐I as potential atheroprotective agents</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>Amphipathic α‐Helical Peptide Models of ApoA‐I</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Conformational study of new amphipathic α‐helical peptide models of apoA‐I as potential atheroprotective agents</title></titleInfo><name type="personal"><namePart type="given">Chrystel</namePart><namePart type="family">Beaufils</namePart><affiliation>Laboratoire de Chimie‐Physique Macromoléculaire, UMR 7568 CNRS‐INPL, ENSIC, 1 rue Grandville, B.P. 20451, 54001 Nancy Cedex, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Charalampos</namePart><namePart type="family">Alexopoulos</namePart><affiliation>Department of Chemistry, University of Ioannina, Box 1186, 451 10 Ioannina, Greece</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Maria P.</namePart><namePart type="family">Petraki</namePart><affiliation>Department of Chemistry, University of Ioannina, Box 1186, 451 10 Ioannina, Greece</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Alexandros D.</namePart><namePart type="family">Tselepis</namePart><affiliation>Department of Chemistry, University of Ioannina, Box 1186, 451 10 Ioannina, Greece</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Nicolas</namePart><namePart type="family">Coudevylle</namePart><affiliation>Laboratoire de Chimie‐Physique Macromoléculaire, UMR 7568 CNRS‐INPL, ENSIC, 1 rue Grandville, B.P. 20451, 54001 Nancy Cedex, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Maria</namePart><namePart type="family">Sakarellos‐Daitsiotis</namePart><affiliation>Department of Chemistry, University of Ioannina, Box 1186, 451 10 Ioannina, Greece</affiliation><affiliation>E-mail: msakarel@uoi.gr</affiliation><affiliation>Maria Sakarellos‐Daitsiotis, Department of Chemistry, University of Ioannina, Box 1186, 451 10 Ioannina, GreeceManh Thong Cung, Laboratoire de Chimie‐Physique Macromoléculaire, UMR 7568 CNRS‐INPL, ENSIC, 1 rue Grandville, B.P. 20451, 54001 Nancy Cedex, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Constantinos</namePart><namePart type="family">Sakarellos</namePart><affiliation>Department of Chemistry, University of Ioannina, Box 1186, 451 10 Ioannina, Greece</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Manh Thong</namePart><namePart type="family">Cung</namePart><affiliation>Laboratoire de Chimie‐Physique Macromoléculaire, UMR 7568 CNRS‐INPL, ENSIC, 1 rue Grandville, B.P. 20451, 54001 Nancy Cedex, France</affiliation><affiliation>E-mail: manh‐thong.cung@ensic.inpl‐nancy.fr</affiliation><affiliation>Maria Sakarellos‐Daitsiotis, Department of Chemistry, University of Ioannina, Box 1186, 451 10 Ioannina, GreeceManh Thong Cung, Laboratoire de Chimie‐Physique Macromoléculaire, UMR 7568 CNRS‐INPL, ENSIC, 1 rue Grandville, B.P. 20451, 54001 Nancy Cedex, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-6N5SZHKN-D">article</genre><originInfo><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><place><placeTerm type="text">Hoboken</placeTerm></place><dateIssued encoding="w3cdtf">2007</dateIssued><dateCaptured encoding="w3cdtf">2006-07-21</dateCaptured><dateValid encoding="w3cdtf">2006-12-05</dateValid><copyrightDate encoding="w3cdtf">2007</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><extent unit="figures">8</extent><extent unit="tables">3</extent><extent unit="references">50</extent><extent unit="words">9493</extent></physicalDescription><abstract lang="en">Aiming at contributing to the development of potential atheroprotective agents, we report on the concept and design of two peptide models, which mimic the amphipathic helices of apoA‐I and incorporate Met into their sequences to validate its role as oxidant scavenger: Ac‐ESK(Palm)KELSKSW10SEM13LKEK(Palm)SKS‐NH2 (model 1 [W10, M13]) and Ac‐ESK(Palm)KELSKSM10SEW13LKEK(Palm)SKS‐NH2 (model 2 [M10, W13]). Hydrophobic residues of both models cover about the half of the surface, while the positively and negatively charged residues constitute two separate clusters on the hydrophilic face. Palmitoyl groups were introduced into the Lys‐NϵH2 groups at positions 3 and 17 to contribute to the amphipathic character of the peptides and stabilize the nonpolar face of the helix. Conformational study by the combined application of 2D‐NMR and molecular dynamics simulations, CD, FTIR, and fluorescence spectroscopy revealed that model 1 adopts helical conformation and Met is well exposed to the microenvironment. Model 2 that derives from model 1 by exchanging W10 (model 1) with M10 and M13 (model 1) with W13 also displays helical characteristics, while Met is rather shielded. Oxidation experiments indicated that model 1 exhibits a 2‐fold more potent antioxidant activity towards LDL oxidation, compared to model 2, confirming the role of Met, when is devoid of steric hindrances, as oxidant scavenger for the protection of LDL. © 2006 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 88: 362–372, 2007. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com</abstract><note type="funding">Centre National de la Recherche Scientifique</note><note type="funding">EPEAEK (Ministry of Education, Greece)</note><subject lang="en"><genre>keywords</genre><topic>apolipoprotein A‐I</topic><topic>amphipathic α‐helix</topic><topic>atheroprotective peptide models</topic><topic>HDL</topic><topic>LDL</topic><topic>2D‐NMR</topic><topic>NOESY</topic><topic>molecular modeling</topic><topic>CD</topic><topic>fluorescence</topic></subject><relatedItem type="host"><titleInfo><title>Peptide Science</title><subTitle>Original Research on Biomolecules</subTitle></titleInfo><titleInfo type="abbreviated"><title>Biopolymers</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><subject><genre>article-category</genre><topic>Original Research Article</topic></subject><identifier type="ISSN">0006-3525</identifier><identifier type="eISSN">1097-0282</identifier><identifier type="DOI">10.1002/(ISSN)1097-0282a</identifier><identifier type="PublisherID">BIP</identifier><part><date>2007</date><detail type="volume"><caption>vol.</caption><number>88</number></detail><detail type="issue"><caption>no.</caption><number>3</number></detail><extent unit="pages"><start>362</start><end>372</end><total>11</total></extent></part></relatedItem><identifier type="istex">E2DF581AC3537D55048491AF88943DF1F02B76C8</identifier><identifier type="ark">ark:/67375/WNG-DPD0D5R1-3</identifier><identifier type="DOI">10.1002/bip.20651</identifier><identifier type="ArticleID">BIP20651</identifier><accessCondition type="use and reproduction" contentType="copyright">Copyright © 2007 Wiley Periodicals, Inc.</accessCondition><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-L0C46X92-X">wiley</recordContentSource><recordOrigin>Wiley Subscription Services, Inc., A Wiley Company</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/document/E2DF581AC3537D55048491AF88943DF1F02B76C8/metadata/json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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