Conformational requirements for molecular recognition of acetylcholine receptor main immunogenic region (MIR) analogues by monoclonal anti‐MIR antibody: A two‐dimensional nuclear magnetic resonance and molecular dynamics approach
Identifieur interne : 000B35 ( Istex/Corpus ); précédent : 000B34; suivant : 000B36Conformational requirements for molecular recognition of acetylcholine receptor main immunogenic region (MIR) analogues by monoclonal anti‐MIR antibody: A two‐dimensional nuclear magnetic resonance and molecular dynamics approach
Auteurs : Vassilios Tsikaris ; Evangelos Detsikas ; Maria Sakarellos-Daitsiotis ; Constantinos Sakarellos ; Efstratia Vatzaki ; Socrates J. Tzartos ; Michel Marraud ; Manh Thong CungSource :
- Biopolymers [ 0006-3525 ] ; 1993-07.
English descriptors
- KwdEn :
- Achr, Achr fragment, Additional stability, Aib7, Analogue, Analogue decapeptides, Antibody recognition, Aqueous solution, Backbone flexibility, Binding capacity, Chemical shifts, Conformation, Conformational, Conformational behavior, Conformational flexibility, Conformational properties, Connectivity, Constraint, Cung, Decapeptide, Decapeptide analogues, Decapeptide fragment, Decapeptides, Dihedral angle, Distance constraints, Dmso, Dmso solution, Energy minimization, Experimental point, Free state, Heavy line, Intact achr, Interproton distances, John wiley sons, Last period, Mab6, Mab6 antibody, Main immunogenic region, Marraud, Molar ratio, Molecular dynamics, Molecular modeling, More affinity, More flexibility, Natural fragment, Noesy, Noesy connectivities, Noesy experiments, Nonexchangeable protons, Other hand, Peptide, Peptide backbone, Peptide side chains, Previous studies, Proton, Proton resonances, Sakarellos, Side chain, Side chains, Simulation, Solid line, Steric hindrance, Sybyl program, Temperature dependence, Thin line, Tsikaris, Tzartos.
- Teeft :
- Achr, Achr fragment, Additional stability, Aib7, Analogue, Analogue decapeptides, Antibody recognition, Aqueous solution, Backbone flexibility, Binding capacity, Chemical shifts, Conformation, Conformational, Conformational behavior, Conformational flexibility, Conformational properties, Connectivity, Constraint, Cung, Decapeptide, Decapeptide analogues, Decapeptide fragment, Decapeptides, Dihedral angle, Distance constraints, Dmso, Dmso solution, Energy minimization, Experimental point, Free state, Heavy line, Intact achr, Interproton distances, John wiley sons, Last period, Mab6, Mab6 antibody, Main immunogenic region, Marraud, Molar ratio, Molecular dynamics, Molecular modeling, More affinity, More flexibility, Natural fragment, Noesy, Noesy connectivities, Noesy experiments, Nonexchangeable protons, Other hand, Peptide, Peptide backbone, Peptide side chains, Previous studies, Proton, Proton resonances, Sakarellos, Side chain, Side chains, Simulation, Solid line, Steric hindrance, Sybyl program, Temperature dependence, Thin line, Tsikaris, Tzartos.
Abstract
The conformational properties of two [D‐A70, A76] and [Aib70, A76] analogues of the α67–76 Torpedo acetylcholine receptor fragment, with low binding capacity for the anti main immunogenic region (MIR) antibodies, were studied in DMSO by two‐dimensional nmr techniques and molecular dynamics simulations. The results were compared to the free and bound conformations of the [A76] analogue, which has twice more affinity for the anti‐MIR monoclonal antibody 6 (mAb6), than the natural Torpedo sequence. It appeared that a single substitution of the A70, at a crucial position, by the D‐A70 or Aib70, could modify completely the conformational behavior of the peptide and reduced its recognition by the anti‐MIR antibody. The WNPADY rigid structure at the N‐terminal part was essential for antibody recognition. The adjacent more flexible C‐terminal sequence (GGIK) gives additional stability to the monoclonal antibody–peptide complex probably due to an adequate orientation of the peptide side chains in the complex, by setting them in close contact with the antibody. © 1993 John Wiley & Sons, Inc.
Url:
DOI: 10.1002/bip.360330714
Links to Exploration step
ISTEX:5E2CD50C9391393D11E9AD216F0797B80A8A7BF8Le document en format XML
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Tzartos</name><affiliation><mods:affiliation>Department of Biochemistry, Hellenic Pasteur Institute, 127 Vassilissis Sofias Avenue, 115 21 Athens, Greece</mods:affiliation></affiliation></author><author><name sortKey="Marraud, Michel" sort="Marraud, Michel" uniqKey="Marraud M" first="Michel" last="Marraud">Michel Marraud</name><affiliation><mods:affiliation>Laboratoire de Chimie‐Physique Macromoléculaire, CNRS‐URA 494, ENSIC‐INPL, 1 rue Grandville, BP 451, 54001 Nancy Cedex, France</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, CNRS‐URA 494, ENSIC‐INPL, 1 rue Grandville, BP 451, 54001 Nancy Cedex, France</mods:affiliation></affiliation><affiliation><mods:affiliation>Correspondence address: Laboratoire de Chimie‐Physique Macromoléculaire, CNRS‐URA 494, ENSIC‐INPL, 1 rue Grandville, BP 451, 54001 Nancy Cedex, France</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Biopolymers</title><title level="j" type="alt">BIOPOLYMERS</title><idno type="ISSN">0006-3525</idno><idno type="eISSN">1097-0282</idno><imprint><biblScope unit="vol">33</biblScope><biblScope unit="issue">7</biblScope><biblScope unit="page" from="1123">1123</biblScope><biblScope unit="page" to="1134">1134</biblScope><biblScope unit="page-count">12</biblScope><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><date type="published" when="1993-07">1993-07</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>Achr</term><term>Achr fragment</term><term>Additional stability</term><term>Aib7</term><term>Analogue</term><term>Analogue decapeptides</term><term>Antibody recognition</term><term>Aqueous solution</term><term>Backbone flexibility</term><term>Binding capacity</term><term>Chemical shifts</term><term>Conformation</term><term>Conformational</term><term>Conformational behavior</term><term>Conformational flexibility</term><term>Conformational properties</term><term>Connectivity</term><term>Constraint</term><term>Cung</term><term>Decapeptide</term><term>Decapeptide analogues</term><term>Decapeptide fragment</term><term>Decapeptides</term><term>Dihedral angle</term><term>Distance constraints</term><term>Dmso</term><term>Dmso solution</term><term>Energy minimization</term><term>Experimental point</term><term>Free state</term><term>Heavy line</term><term>Intact achr</term><term>Interproton distances</term><term>John wiley sons</term><term>Last period</term><term>Mab6</term><term>Mab6 antibody</term><term>Main immunogenic region</term><term>Marraud</term><term>Molar ratio</term><term>Molecular dynamics</term><term>Molecular modeling</term><term>More affinity</term><term>More flexibility</term><term>Natural fragment</term><term>Noesy</term><term>Noesy connectivities</term><term>Noesy experiments</term><term>Nonexchangeable protons</term><term>Other hand</term><term>Peptide</term><term>Peptide backbone</term><term>Peptide side chains</term><term>Previous studies</term><term>Proton</term><term>Proton resonances</term><term>Sakarellos</term><term>Side chain</term><term>Side chains</term><term>Simulation</term><term>Solid line</term><term>Steric hindrance</term><term>Sybyl program</term><term>Temperature dependence</term><term>Thin line</term><term>Tsikaris</term><term>Tzartos</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Achr</term><term>Achr fragment</term><term>Additional stability</term><term>Aib7</term><term>Analogue</term><term>Analogue decapeptides</term><term>Antibody recognition</term><term>Aqueous solution</term><term>Backbone flexibility</term><term>Binding capacity</term><term>Chemical shifts</term><term>Conformation</term><term>Conformational</term><term>Conformational behavior</term><term>Conformational flexibility</term><term>Conformational properties</term><term>Connectivity</term><term>Constraint</term><term>Cung</term><term>Decapeptide</term><term>Decapeptide analogues</term><term>Decapeptide fragment</term><term>Decapeptides</term><term>Dihedral angle</term><term>Distance constraints</term><term>Dmso</term><term>Dmso solution</term><term>Energy minimization</term><term>Experimental point</term><term>Free state</term><term>Heavy line</term><term>Intact achr</term><term>Interproton distances</term><term>John wiley sons</term><term>Last period</term><term>Mab6</term><term>Mab6 antibody</term><term>Main immunogenic region</term><term>Marraud</term><term>Molar ratio</term><term>Molecular dynamics</term><term>Molecular modeling</term><term>More affinity</term><term>More flexibility</term><term>Natural fragment</term><term>Noesy</term><term>Noesy connectivities</term><term>Noesy experiments</term><term>Nonexchangeable protons</term><term>Other hand</term><term>Peptide</term><term>Peptide backbone</term><term>Peptide side chains</term><term>Previous studies</term><term>Proton</term><term>Proton resonances</term><term>Sakarellos</term><term>Side chain</term><term>Side chains</term><term>Simulation</term><term>Solid line</term><term>Steric hindrance</term><term>Sybyl program</term><term>Temperature dependence</term><term>Thin line</term><term>Tsikaris</term><term>Tzartos</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The conformational properties of two [D‐A70, A76] and [Aib70, A76] analogues of the α67–76 Torpedo acetylcholine receptor fragment, with low binding capacity for the anti main immunogenic region (MIR) antibodies, were studied in DMSO by two‐dimensional nmr techniques and molecular dynamics simulations. The results were compared to the free and bound conformations of the [A76] analogue, which has twice more affinity for the anti‐MIR monoclonal antibody 6 (mAb6), than the natural Torpedo sequence. It appeared that a single substitution of the A70, at a crucial position, by the D‐A70 or Aib70, could modify completely the conformational behavior of the peptide and reduced its recognition by the anti‐MIR antibody. The WNPADY rigid structure at the N‐terminal part was essential for antibody recognition. The adjacent more flexible C‐terminal sequence (GGIK) gives additional stability to the monoclonal antibody–peptide complex probably due to an adequate orientation of the peptide side chains in the complex, by setting them in close contact with the antibody. © 1993 John Wiley & Sons, Inc.</div></front></TEI><istex><corpusName>wiley</corpusName><keywords><teeft><json:string>aib7</json:string><json:string>analogue</json:string><json:string>achr</json:string><json:string>mab6</json:string><json:string>peptide</json:string><json:string>side chains</json:string><json:string>decapeptide</json:string><json:string>tzartos</json:string><json:string>noesy</json:string><json:string>tsikaris</json:string><json:string>marraud</json:string><json:string>decapeptides</json:string><json:string>cung</json:string><json:string>dmso</json:string><json:string>side chain</json:string><json:string>connectivity</json:string><json:string>sakarellos</json:string><json:string>distance constraints</json:string><json:string>peptide backbone</json:string><json:string>interproton distances</json:string><json:string>conformation</json:string><json:string>conformational behavior</json:string><json:string>achr fragment</json:string><json:string>antibody recognition</json:string><json:string>aqueous solution</json:string><json:string>conformational</json:string><json:string>simulation</json:string><json:string>free state</json:string><json:string>binding capacity</json:string><json:string>chemical shifts</json:string><json:string>john wiley sons</json:string><json:string>mab6 antibody</json:string><json:string>constraint</json:string><json:string>proton</json:string><json:string>last period</json:string><json:string>noesy experiments</json:string><json:string>previous studies</json:string><json:string>sybyl program</json:string><json:string>molecular dynamics</json:string><json:string>decapeptide analogues</json:string><json:string>intact achr</json:string><json:string>molecular modeling</json:string><json:string>decapeptide fragment</json:string><json:string>more flexibility</json:string><json:string>dmso solution</json:string><json:string>proton resonances</json:string><json:string>other hand</json:string><json:string>energy minimization</json:string><json:string>temperature dependence</json:string><json:string>dihedral angle</json:string><json:string>main immunogenic region</json:string><json:string>analogue decapeptides</json:string><json:string>noesy connectivities</json:string><json:string>experimental point</json:string><json:string>solid line</json:string><json:string>conformational properties</json:string><json:string>backbone flexibility</json:string><json:string>steric hindrance</json:string><json:string>peptide side chains</json:string><json:string>conformational flexibility</json:string><json:string>molar ratio</json:string><json:string>natural fragment</json:string><json:string>nonexchangeable protons</json:string><json:string>heavy line</json:string><json:string>thin line</json:string><json:string>additional stability</json:string><json:string>more affinity</json:string></teeft></keywords><author><json:item><name>Vassilios Tsikaris</name><affiliations><json:string>Department of Chemistry, University of loannina, Box 1186, 451 10 loannina, Greece</json:string></affiliations></json:item><json:item><name>Evangelos Detsikas</name><affiliations><json:string>Department of Chemistry, University of loannina, Box 1186, 451 10 loannina, Greece</json:string></affiliations></json:item><json:item><name>Maria Sakarellos‐Daitsiotis</name><affiliations><json:string>Department of Chemistry, University of loannina, Box 1186, 451 10 loannina, Greece</json:string></affiliations></json:item><json:item><name>Constantinos Sakarellos</name><affiliations><json:string>Department of Chemistry, University of loannina, Box 1186, 451 10 loannina, Greece</json:string></affiliations></json:item><json:item><name>Efstratia Vatzaki</name><affiliations><json:string>Department of Biochemistry, Hellenic Pasteur Institute, 127 Vassilissis Sofias Avenue, 115 21 Athens, Greece</json:string></affiliations></json:item><json:item><name>Socrates J. Tzartos</name><affiliations><json:string>Department of Biochemistry, Hellenic Pasteur Institute, 127 Vassilissis Sofias Avenue, 115 21 Athens, Greece</json:string></affiliations></json:item><json:item><name>Michel Marraud</name><affiliations><json:string>Laboratoire de Chimie‐Physique Macromoléculaire, CNRS‐URA 494, ENSIC‐INPL, 1 rue Grandville, BP 451, 54001 Nancy Cedex, France</json:string></affiliations></json:item><json:item><name>Manh Thong Cung</name><affiliations><json:string>Laboratoire de Chimie‐Physique Macromoléculaire, CNRS‐URA 494, ENSIC‐INPL, 1 rue Grandville, BP 451, 54001 Nancy Cedex, France</json:string><json:string>Laboratoire de Chimie‐Physique Macromoléculaire, CNRS‐URA 494, ENSIC‐INPL, 1 rue Grandville, BP 451, 54001 Nancy Cedex, France</json:string></affiliations></json:item></author><articleId><json:string>BIP360330714</json:string></articleId><language><json:string>eng</json:string></language><originalGenre><json:string>article</json:string></originalGenre><abstract>The conformational properties of two [D‐A70, A76] and [Aib70, A76] analogues of the α67–76 Torpedo acetylcholine receptor fragment, with low binding capacity for the anti main immunogenic region (MIR) antibodies, were studied in DMSO by two‐dimensional nmr techniques and molecular dynamics simulations. The results were compared to the free and bound conformations of the [A76] analogue, which has twice more affinity for the anti‐MIR monoclonal antibody 6 (mAb6), than the natural Torpedo sequence. It appeared that a single substitution of the A70, at a crucial position, by the D‐A70 or Aib70, could modify completely the conformational behavior of the peptide and reduced its recognition by the anti‐MIR antibody. The WNPADY rigid structure at the N‐terminal part was essential for antibody recognition. The adjacent more flexible C‐terminal sequence (GGIK) gives additional stability to the monoclonal antibody–peptide complex probably due to an adequate orientation of the peptide side chains in the complex, by setting them in close contact with the antibody. © 1993 John Wiley & Sons, Inc.</abstract><qualityIndicators><score>6.789</score><pdfVersion>1.3</pdfVersion><pdfPageSize>612 x 810 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractCharCount>1098</abstractCharCount><pdfWordCount>4797</pdfWordCount><pdfCharCount>30680</pdfCharCount><pdfPageCount>12</pdfPageCount><abstractWordCount>166</abstractWordCount></qualityIndicators><title>Conformational requirements for molecular recognition of acetylcholine receptor main immunogenic region (MIR) analogues by monoclonal anti‐MIR antibody: A two‐dimensional nuclear magnetic resonance and molecular dynamics 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uri="https://api.istex.fr/document/5E2CD50C9391393D11E9AD216F0797B80A8A7BF8/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">Conformational requirements for molecular recognition of acetylcholine receptor main immunogenic region (MIR) analogues by monoclonal anti‐MIR antibody: A two‐dimensional nuclear magnetic resonance and molecular dynamics approach</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><availability><licence>Copyright © 1993 John Wiley & Sons, Inc.</licence></availability><date type="published" when="1993-07"></date></publicationStmt><notesStmt><note type="content-type" subtype="article" source="article" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-6N5SZHKN-D">article</note><note type="publication-type" subtype="journal" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note></notesStmt><sourceDesc><biblStruct type="article"><analytic><title level="a" type="main" xml:lang="en">Conformational requirements for molecular recognition of acetylcholine receptor main immunogenic region (MIR) analogues by monoclonal anti‐MIR antibody: A two‐dimensional nuclear magnetic resonance and molecular dynamics approach</title><title level="a" type="short" xml:lang="en">RECOGNITION OF ACHR MIR ANALOGUES</title><author xml:id="author-0000"><persName><forename type="first">Vassilios</forename><surname>Tsikaris</surname></persName><affiliation>Department of Chemistry, University of loannina, Box 1186, 451 10 loannina, Greece<address><country key="GR"></country></address></affiliation></author><author xml:id="author-0001"><persName><forename type="first">Evangelos</forename><surname>Detsikas</surname></persName><affiliation>Department of Chemistry, University of loannina, Box 1186, 451 10 loannina, Greece<address><country key="GR"></country></address></affiliation></author><author xml:id="author-0002"><persName><forename type="first">Maria</forename><surname>Sakarellos‐Daitsiotis</surname></persName><affiliation>Department of Chemistry, University of loannina, Box 1186, 451 10 loannina, Greece<address><country key="GR"></country></address></affiliation></author><author xml:id="author-0003"><persName><forename type="first">Constantinos</forename><surname>Sakarellos</surname></persName><affiliation>Department of Chemistry, University of loannina, Box 1186, 451 10 loannina, Greece<address><country key="GR"></country></address></affiliation></author><author xml:id="author-0004"><persName><forename type="first">Efstratia</forename><surname>Vatzaki</surname></persName><affiliation>Department of Biochemistry, Hellenic Pasteur Institute, 127 Vassilissis Sofias Avenue, 115 21 Athens, Greece<address><country key="GR"></country></address></affiliation></author><author xml:id="author-0005"><persName><forename type="first">Socrates J.</forename><surname>Tzartos</surname></persName><affiliation>Department of Biochemistry, Hellenic Pasteur Institute, 127 Vassilissis Sofias Avenue, 115 21 Athens, Greece<address><country key="GR"></country></address></affiliation></author><author xml:id="author-0006"><persName><forename type="first">Michel</forename><surname>Marraud</surname></persName><affiliation>Laboratoire de Chimie‐Physique Macromoléculaire, CNRS‐URA 494, ENSIC‐INPL, 1 rue Grandville, BP 451, 54001 Nancy Cedex, France<address><country key="FR"></country></address></affiliation></author><author xml:id="author-0007" role="corresp"><persName><forename type="first">Manh Thong</forename><surname>Cung</surname></persName><affiliation>Laboratoire de Chimie‐Physique Macromoléculaire, CNRS‐URA 494, ENSIC‐INPL, 1 rue Grandville, BP 451, 54001 Nancy Cedex, France<address><country key="FR"></country></address></affiliation><affiliation>Laboratoire de Chimie‐Physique Macromoléculaire, CNRS‐URA 494, ENSIC‐INPL, 1 rue Grandville, BP 451, 54001 Nancy Cedex, France</affiliation></author><idno type="istex">5E2CD50C9391393D11E9AD216F0797B80A8A7BF8</idno><idno type="ark">ark:/67375/WNG-RQ3NWJDW-F</idno><idno type="DOI">10.1002/bip.360330714</idno><idno type="unit">BIP360330714</idno><idno type="toTypesetVersion">file:BIP.BIP360330714.pdf</idno></analytic><monogr><title level="j" type="main">Biopolymers</title><title level="j" type="alt">BIOPOLYMERS</title><idno type="pISSN">0006-3525</idno><idno type="eISSN">1097-0282</idno><idno type="book-DOI">10.1002/(ISSN)1097-0282</idno><idno type="book-part-DOI">10.1002/bip.v33:7</idno><idno type="product">BIP</idno><imprint><biblScope unit="vol">33</biblScope><biblScope unit="issue">7</biblScope><biblScope unit="page" from="1123">1123</biblScope><biblScope unit="page" to="1134">1134</biblScope><biblScope unit="page-count">12</biblScope><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><date type="published" when="1993-07"></date></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><abstract xml:lang="en" style="main"><head>Abstract</head><p>The conformational properties of two [<hi rend="smallCaps">D</hi>‐A<hi rend="superscript">70</hi>, A<hi rend="superscript">76</hi>] and [Aib<hi rend="superscript">70</hi>, A<hi rend="superscript">76</hi>] analogues of the α67–76 <hi rend="italic">Torpedo</hi> acetylcholine receptor fragment, with low binding capacity for the anti main immunogenic region (MIR) antibodies, were studied in DMSO by two‐dimensional nmr techniques and molecular dynamics simulations. The results were compared to the free and bound conformations of the [A<hi rend="superscript">76</hi>] analogue, which has twice more affinity for the anti‐MIR monoclonal antibody 6 (mAb6), than the natural <hi rend="italic">Torpedo</hi> sequence. It appeared that a single substitution of the A<hi rend="superscript">70</hi>, at a crucial position, by the <hi rend="smallCaps">D</hi>‐A<hi rend="superscript">70</hi> or Aib<hi rend="superscript">70</hi>, could modify completely the conformational behavior of the peptide and reduced its recognition by the anti‐MIR antibody. The WNPADY rigid structure at the N‐terminal part was essential for antibody recognition. The adjacent more flexible C‐terminal sequence (GGIK) gives additional stability to the monoclonal antibody–peptide complex probably due to an adequate orientation of the peptide side chains in the complex, by setting them in close contact with the antibody. © 1993 John Wiley & Sons, Inc.</p></abstract><textClass><keywords rend="articleCategory"><term>Article</term></keywords><keywords rend="tocHeading1"><term>Articles</term></keywords></textClass><langUsage><language ident="en"></language></langUsage></profileDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/document/5E2CD50C9391393D11E9AD216F0797B80A8A7BF8/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Wiley, elements deleted: body"><istex:xmlDeclaration>version="1.0" encoding="UTF-8" standalone="yes"</istex:xmlDeclaration><istex:document><component version="2.0" type="serialArticle" 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xml:id="au1" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Vassilios</givenNames><familyName>Tsikaris</familyName></personName></creator><creator xml:id="au2" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Evangelos</givenNames><familyName>Detsikas</familyName></personName></creator><creator xml:id="au3" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Maria</givenNames><familyName>Sakarellos‐Daitsiotis</familyName></personName></creator><creator xml:id="au4" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Constantinos</givenNames><familyName>Sakarellos</familyName></personName></creator><creator xml:id="au5" creatorRole="author" affiliationRef="#af2"><personName><givenNames>Efstratia</givenNames><familyName>Vatzaki</familyName></personName></creator><creator xml:id="au6" creatorRole="author" affiliationRef="#af2"><personName><givenNames>Socrates J.</givenNames><familyName>Tzartos</familyName></personName></creator><creator xml:id="au7" creatorRole="author" affiliationRef="#af3"><personName><givenNames>Michel</givenNames><familyName>Marraud</familyName></personName></creator><creator xml:id="au8" creatorRole="author" affiliationRef="#af3" corresponding="yes"><personName><givenNames>Manh Thong</givenNames><familyName>Cung</familyName></personName></creator></creators><affiliationGroup><affiliation xml:id="af1" countryCode="GR" type="organization"><unparsedAffiliation>Department of Chemistry, University of loannina, Box 1186, 451 10 loannina, Greece</unparsedAffiliation></affiliation><affiliation xml:id="af2" countryCode="GR" type="organization"><unparsedAffiliation>Department of Biochemistry, Hellenic Pasteur Institute, 127 Vassilissis Sofias Avenue, 115 21 Athens, Greece</unparsedAffiliation></affiliation><affiliation xml:id="af3" countryCode="FR" type="organization"><unparsedAffiliation>Laboratoire de Chimie‐Physique Macromoléculaire, CNRS‐URA 494, ENSIC‐INPL, 1 rue Grandville, BP 451, 54001 Nancy Cedex, France</unparsedAffiliation></affiliation></affiliationGroup><abstractGroup><abstract type="main" xml:lang="en"><title type="main">Abstract</title><p>The conformational properties of two [<sc>D</sc>‐A<sup>70</sup>, A<sup>76</sup>] and [Aib<sup>70</sup>, A<sup>76</sup>] analogues of the α67–76 <i>Torpedo</i> acetylcholine receptor fragment, with low binding capacity for the anti main immunogenic region (MIR) antibodies, were studied in DMSO by two‐dimensional nmr techniques and molecular dynamics simulations. The results were compared to the free and bound conformations of the [A<sup>76</sup>] analogue, which has twice more affinity for the anti‐MIR monoclonal antibody 6 (mAb6), than the natural <i>Torpedo</i> sequence. It appeared that a single substitution of the A<sup>70</sup>, at a crucial position, by the <sc>D</sc>‐A<sup>70</sup> or Aib<sup>70</sup>, could modify completely the conformational behavior of the peptide and reduced its recognition by the anti‐MIR antibody. The WNPADY rigid structure at the N‐terminal part was essential for antibody recognition. The adjacent more flexible C‐terminal sequence (GGIK) gives additional stability to the monoclonal antibody–peptide complex probably due to an adequate orientation of the peptide side chains in the complex, by setting them in close contact with the antibody. © 1993 John Wiley & Sons, Inc.</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Conformational requirements for molecular recognition of acetylcholine receptor main immunogenic region (MIR) analogues by monoclonal anti‐MIR antibody: A two‐dimensional nuclear magnetic resonance and molecular dynamics approach</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>RECOGNITION OF ACHR MIR ANALOGUES</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Conformational requirements for molecular recognition of acetylcholine receptor main immunogenic region (MIR) analogues by monoclonal anti‐MIR antibody: A two‐dimensional nuclear magnetic resonance and molecular dynamics approach</title></titleInfo><name type="personal"><namePart type="given">Vassilios</namePart><namePart type="family">Tsikaris</namePart><affiliation>Department of Chemistry, University of loannina, Box 1186, 451 10 loannina, Greece</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Evangelos</namePart><namePart type="family">Detsikas</namePart><affiliation>Department of Chemistry, University of loannina, Box 1186, 451 10 loannina, Greece</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 loannina, Box 1186, 451 10 loannina, Greece</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 loannina, Box 1186, 451 10 loannina, Greece</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Efstratia</namePart><namePart type="family">Vatzaki</namePart><affiliation>Department of Biochemistry, Hellenic Pasteur Institute, 127 Vassilissis Sofias Avenue, 115 21 Athens, Greece</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Socrates J.</namePart><namePart type="family">Tzartos</namePart><affiliation>Department of Biochemistry, Hellenic Pasteur Institute, 127 Vassilissis Sofias Avenue, 115 21 Athens, Greece</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Michel</namePart><namePart type="family">Marraud</namePart><affiliation>Laboratoire de Chimie‐Physique Macromoléculaire, CNRS‐URA 494, ENSIC‐INPL, 1 rue Grandville, BP 451, 54001 Nancy Cedex, France</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, CNRS‐URA 494, ENSIC‐INPL, 1 rue Grandville, BP 451, 54001 Nancy Cedex, France</affiliation><affiliation>Correspondence address: Laboratoire de Chimie‐Physique Macromoléculaire, CNRS‐URA 494, ENSIC‐INPL, 1 rue Grandville, BP 451, 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">1993-07</dateIssued><dateCaptured encoding="w3cdtf">1992-08-08</dateCaptured><dateValid encoding="w3cdtf">1992-12-05</dateValid><copyrightDate encoding="w3cdtf">1993</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><extent unit="figures">4</extent><extent unit="tables">7</extent><extent unit="references">25</extent></physicalDescription><abstract lang="en">The conformational properties of two [D‐A70, A76] and [Aib70, A76] analogues of the α67–76 Torpedo acetylcholine receptor fragment, with low binding capacity for the anti main immunogenic region (MIR) antibodies, were studied in DMSO by two‐dimensional nmr techniques and molecular dynamics simulations. The results were compared to the free and bound conformations of the [A76] analogue, which has twice more affinity for the anti‐MIR monoclonal antibody 6 (mAb6), than the natural Torpedo sequence. It appeared that a single substitution of the A70, at a crucial position, by the D‐A70 or Aib70, could modify completely the conformational behavior of the peptide and reduced its recognition by the anti‐MIR antibody. The WNPADY rigid structure at the N‐terminal part was essential for antibody recognition. The adjacent more flexible C‐terminal sequence (GGIK) gives additional stability to the monoclonal antibody–peptide complex probably due to an adequate orientation of the peptide side chains in the complex, by setting them in close contact with the antibody. © 1993 John Wiley & Sons, Inc.</abstract><relatedItem type="host"><titleInfo><title>Biopolymers</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>Article</topic></subject><identifier type="ISSN">0006-3525</identifier><identifier type="eISSN">1097-0282</identifier><identifier type="DOI">10.1002/(ISSN)1097-0282</identifier><identifier type="PublisherID">BIP</identifier><part><date>1993</date><detail type="volume"><caption>vol.</caption><number>33</number></detail><detail type="issue"><caption>no.</caption><number>7</number></detail><extent unit="pages"><start>1123</start><end>1134</end><total>12</total></extent></part></relatedItem><identifier type="istex">5E2CD50C9391393D11E9AD216F0797B80A8A7BF8</identifier><identifier type="ark">ark:/67375/WNG-RQ3NWJDW-F</identifier><identifier type="DOI">10.1002/bip.360330714</identifier><identifier type="ArticleID">BIP360330714</identifier><accessCondition type="use and reproduction" contentType="copyright">Copyright © 1993 John Wiley & Sons, 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/5E2CD50C9391393D11E9AD216F0797B80A8A7BF8/metadata/json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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