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
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<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>
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<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>
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<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>
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<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>
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<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>
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<titleInfo type="abbreviated" lang="en"><title>Amphipathic α‐Helical Peptide Models of ApoA‐I</title>
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<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>
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<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>
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<name type="personal"><namePart type="given">Charalampos</namePart>
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<affiliation>Department of Chemistry, University of Ioannina, Box 1186, 451 10 Ioannina, Greece</affiliation>
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<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>
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<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>
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<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>
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<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>
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<name type="personal"><namePart type="given">Manh Thong</namePart>
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<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>
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<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>
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<topic>apolipoprotein A‐I</topic>
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<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>
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<identifier type="ISSN">0006-3525</identifier>
<identifier type="eISSN">1097-0282</identifier>
<identifier type="DOI">10.1002/(ISSN)1097-0282a</identifier>
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<part><date>2007</date>
<detail type="volume"><caption>vol.</caption>
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