Design, synthesis, and conformational study of biologically active photolabeled analogues of the main immunogenic region of the acetylcholine receptor.
Identifieur interne : 002542 ( PubMed/Curation ); précédent : 002541; suivant : 002543Design, synthesis, and conformational study of biologically active photolabeled analogues of the main immunogenic region of the acetylcholine receptor.
Auteurs : V. Theodorou [Grèce] ; V. Tsikaris ; M. Sakarellos-Daitsiotis ; V. Avramopoulou ; K. Kostelidou ; S J Tzartos ; C. SakarellosSource :
- Biopolymers [ 0006-3525 ]
Descripteurs français
- KwdFr :
- Animaux, Anticorps monoclonaux, Conception de médicament, Conformation des protéines, Fragments peptidiques (), Fragments peptidiques (immunologie), Fragments peptidiques (synthèse chimique), Humains, Immunochimie, Marqueurs d'affinité (), Marqueurs d'affinité (synthèse chimique), Oligopeptides (), Oligopeptides (immunologie), Oligopeptides (synthèse chimique), Photochimie, Récepteurs nicotiniques (), Récepteurs nicotiniques (immunologie), Sites de fixation, Spectroscopie par résonance magnétique, Séquence d'acides aminés, Techniques in vitro.
- MESH :
- immunologie : Fragments peptidiques, Oligopeptides, Récepteurs nicotiniques.
- synthèse chimique : Fragments peptidiques, Marqueurs d'affinité, Oligopeptides.
- Animaux, Anticorps monoclonaux, Conception de médicament, Conformation des protéines, Fragments peptidiques, Humains, Immunochimie, Marqueurs d'affinité, Oligopeptides, Photochimie, Récepteurs nicotiniques, Sites de fixation, Spectroscopie par résonance magnétique, Séquence d'acides aminés, Techniques in vitro.
English descriptors
- KwdEn :
- Affinity Labels (chemical synthesis), Affinity Labels (chemistry), Amino Acid Sequence, Animals, Antibodies, Monoclonal, Binding Sites, Drug Design, Humans, Immunochemistry, In Vitro Techniques, Magnetic Resonance Spectroscopy, Oligopeptides (chemical synthesis), Oligopeptides (chemistry), Oligopeptides (immunology), Peptide Fragments (chemical synthesis), Peptide Fragments (chemistry), Peptide Fragments (immunology), Photochemistry, Protein Conformation, Receptors, Nicotinic (chemistry), Receptors, Nicotinic (immunology).
- MESH :
- chemical , chemical synthesis : Affinity Labels, Oligopeptides, Peptide Fragments.
- chemical , chemistry : Affinity Labels, Oligopeptides, Peptide Fragments, Receptors, Nicotinic.
- chemical , immunology : Oligopeptides, Peptide Fragments, Receptors, Nicotinic.
- Amino Acid Sequence, Animals, Antibodies, Monoclonal, Binding Sites, Drug Design, Humans, Immunochemistry, In Vitro Techniques, Magnetic Resonance Spectroscopy, Photochemistry, Protein Conformation.
Abstract
Photoaffinity labeling is a powerful tool for the characterization of the molecular basis of ligand binding to acceptor molecules, which provides important insights for mapping the bimolecular interfaces. The autoimmune disease myasthenia gravis is caused by autoantibodies against the acetylcholine receptor (AChR). The majority of the anti-AChR antibodies bind to the "main immunogenic region" (MIR) of the AChR. To identify the contact points between the complementarity determining regions of the anti-MIR antibodies that recognize the MIR contact sites of the AChR, we present here three photoreactive dodecapeptide MIR analogues containing the photolabel p-benzoyl-L-phenylalanine (Bpa) moiety, either in position 1 or 11. The structure of the produced 12-mers was analyzed using two-dimensional (1)H-NMR spectroscopy, whereas their binding to anti-MIR monoclonal antibodies (mAbs) was determined by immunochemical assays. In all cases the modifications resulted in conservation of the beta-turn conformation of the N-terminus, which has been proved essential for antibody recognition and increased anti-MIR binding relative to the MIR decapeptide.
DOI: 10.1002/1097-0282(2000)56:1<37::AID-BIP1041>3.0.CO;2-X
PubMed: 11582576
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: Pour aller vers cette notice dans l'étape Curation :002542
Links to Exploration step
pubmed:11582576Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Design, synthesis, and conformational study of biologically active photolabeled analogues of the main immunogenic region of the acetylcholine receptor.</title>
<author><name sortKey="Theodorou, V" sort="Theodorou, V" uniqKey="Theodorou V" first="V" last="Theodorou">V. Theodorou</name>
<affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, University of Ioannina, 45 110 Ioannina, Greece.</nlm:affiliation>
<country xml:lang="fr">Grèce</country>
<wicri:regionArea>Department of Chemistry, University of Ioannina, 45 110 Ioannina</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Tsikaris, V" sort="Tsikaris, V" uniqKey="Tsikaris V" first="V" last="Tsikaris">V. Tsikaris</name>
</author>
<author><name sortKey="Sakarellos Daitsiotis, M" sort="Sakarellos Daitsiotis, M" uniqKey="Sakarellos Daitsiotis M" first="M" last="Sakarellos-Daitsiotis">M. Sakarellos-Daitsiotis</name>
</author>
<author><name sortKey="Avramopoulou, V" sort="Avramopoulou, V" uniqKey="Avramopoulou V" first="V" last="Avramopoulou">V. Avramopoulou</name>
</author>
<author><name sortKey="Kostelidou, K" sort="Kostelidou, K" uniqKey="Kostelidou K" first="K" last="Kostelidou">K. Kostelidou</name>
</author>
<author><name sortKey="Tzartos, S J" sort="Tzartos, S J" uniqKey="Tzartos S" first="S J" last="Tzartos">S J Tzartos</name>
</author>
<author><name sortKey="Sakarellos, C" sort="Sakarellos, C" uniqKey="Sakarellos C" first="C" last="Sakarellos">C. Sakarellos</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="????"><PubDate><MedlineDate>2000-2001</MedlineDate>
</PubDate>
</date>
<idno type="RBID">pubmed:11582576</idno>
<idno type="pmid">11582576</idno>
<idno type="doi">10.1002/1097-0282(2000)56:1<37::AID-BIP1041>3.0.CO;2-X</idno>
<idno type="wicri:Area/PubMed/Corpus">002542</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002542</idno>
<idno type="wicri:Area/PubMed/Curation">002542</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002542</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Design, synthesis, and conformational study of biologically active photolabeled analogues of the main immunogenic region of the acetylcholine receptor.</title>
<author><name sortKey="Theodorou, V" sort="Theodorou, V" uniqKey="Theodorou V" first="V" last="Theodorou">V. Theodorou</name>
<affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, University of Ioannina, 45 110 Ioannina, Greece.</nlm:affiliation>
<country xml:lang="fr">Grèce</country>
<wicri:regionArea>Department of Chemistry, University of Ioannina, 45 110 Ioannina</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Tsikaris, V" sort="Tsikaris, V" uniqKey="Tsikaris V" first="V" last="Tsikaris">V. Tsikaris</name>
</author>
<author><name sortKey="Sakarellos Daitsiotis, M" sort="Sakarellos Daitsiotis, M" uniqKey="Sakarellos Daitsiotis M" first="M" last="Sakarellos-Daitsiotis">M. Sakarellos-Daitsiotis</name>
</author>
<author><name sortKey="Avramopoulou, V" sort="Avramopoulou, V" uniqKey="Avramopoulou V" first="V" last="Avramopoulou">V. Avramopoulou</name>
</author>
<author><name sortKey="Kostelidou, K" sort="Kostelidou, K" uniqKey="Kostelidou K" first="K" last="Kostelidou">K. Kostelidou</name>
</author>
<author><name sortKey="Tzartos, S J" sort="Tzartos, S J" uniqKey="Tzartos S" first="S J" last="Tzartos">S J Tzartos</name>
</author>
<author><name sortKey="Sakarellos, C" sort="Sakarellos, C" uniqKey="Sakarellos C" first="C" last="Sakarellos">C. Sakarellos</name>
</author>
</analytic>
<series><title level="j">Biopolymers</title>
<idno type="ISSN">0006-3525</idno>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Affinity Labels (chemical synthesis)</term>
<term>Affinity Labels (chemistry)</term>
<term>Amino Acid Sequence</term>
<term>Animals</term>
<term>Antibodies, Monoclonal</term>
<term>Binding Sites</term>
<term>Drug Design</term>
<term>Humans</term>
<term>Immunochemistry</term>
<term>In Vitro Techniques</term>
<term>Magnetic Resonance Spectroscopy</term>
<term>Oligopeptides (chemical synthesis)</term>
<term>Oligopeptides (chemistry)</term>
<term>Oligopeptides (immunology)</term>
<term>Peptide Fragments (chemical synthesis)</term>
<term>Peptide Fragments (chemistry)</term>
<term>Peptide Fragments (immunology)</term>
<term>Photochemistry</term>
<term>Protein Conformation</term>
<term>Receptors, Nicotinic (chemistry)</term>
<term>Receptors, Nicotinic (immunology)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term>
<term>Anticorps monoclonaux</term>
<term>Conception de médicament</term>
<term>Conformation des protéines</term>
<term>Fragments peptidiques ()</term>
<term>Fragments peptidiques (immunologie)</term>
<term>Fragments peptidiques (synthèse chimique)</term>
<term>Humains</term>
<term>Immunochimie</term>
<term>Marqueurs d'affinité ()</term>
<term>Marqueurs d'affinité (synthèse chimique)</term>
<term>Oligopeptides ()</term>
<term>Oligopeptides (immunologie)</term>
<term>Oligopeptides (synthèse chimique)</term>
<term>Photochimie</term>
<term>Récepteurs nicotiniques ()</term>
<term>Récepteurs nicotiniques (immunologie)</term>
<term>Sites de fixation</term>
<term>Spectroscopie par résonance magnétique</term>
<term>Séquence d'acides aminés</term>
<term>Techniques in vitro</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemical synthesis" xml:lang="en"><term>Affinity Labels</term>
<term>Oligopeptides</term>
<term>Peptide Fragments</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Affinity Labels</term>
<term>Oligopeptides</term>
<term>Peptide Fragments</term>
<term>Receptors, Nicotinic</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Oligopeptides</term>
<term>Peptide Fragments</term>
<term>Receptors, Nicotinic</term>
</keywords>
<keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Fragments peptidiques</term>
<term>Oligopeptides</term>
<term>Récepteurs nicotiniques</term>
</keywords>
<keywords scheme="MESH" qualifier="synthèse chimique" xml:lang="fr"><term>Fragments peptidiques</term>
<term>Marqueurs d'affinité</term>
<term>Oligopeptides</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Animals</term>
<term>Antibodies, Monoclonal</term>
<term>Binding Sites</term>
<term>Drug Design</term>
<term>Humans</term>
<term>Immunochemistry</term>
<term>In Vitro Techniques</term>
<term>Magnetic Resonance Spectroscopy</term>
<term>Photochemistry</term>
<term>Protein Conformation</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Anticorps monoclonaux</term>
<term>Conception de médicament</term>
<term>Conformation des protéines</term>
<term>Fragments peptidiques</term>
<term>Humains</term>
<term>Immunochimie</term>
<term>Marqueurs d'affinité</term>
<term>Oligopeptides</term>
<term>Photochimie</term>
<term>Récepteurs nicotiniques</term>
<term>Sites de fixation</term>
<term>Spectroscopie par résonance magnétique</term>
<term>Séquence d'acides aminés</term>
<term>Techniques in vitro</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Photoaffinity labeling is a powerful tool for the characterization of the molecular basis of ligand binding to acceptor molecules, which provides important insights for mapping the bimolecular interfaces. The autoimmune disease myasthenia gravis is caused by autoantibodies against the acetylcholine receptor (AChR). The majority of the anti-AChR antibodies bind to the "main immunogenic region" (MIR) of the AChR. To identify the contact points between the complementarity determining regions of the anti-MIR antibodies that recognize the MIR contact sites of the AChR, we present here three photoreactive dodecapeptide MIR analogues containing the photolabel p-benzoyl-L-phenylalanine (Bpa) moiety, either in position 1 or 11. The structure of the produced 12-mers was analyzed using two-dimensional (1)H-NMR spectroscopy, whereas their binding to anti-MIR monoclonal antibodies (mAbs) was determined by immunochemical assays. In all cases the modifications resulted in conservation of the beta-turn conformation of the N-terminus, which has been proved essential for antibody recognition and increased anti-MIR binding relative to the MIR decapeptide.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11582576</PMID>
<DateCompleted><Year>2002</Year>
<Month>02</Month>
<Day>26</Day>
</DateCompleted>
<DateRevised><Year>2014</Year>
<Month>11</Month>
<Day>20</Day>
</DateRevised>
<Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-3525</ISSN>
<JournalIssue CitedMedium="Print"><Volume>56</Volume>
<Issue>1</Issue>
<PubDate><MedlineDate>2000-2001</MedlineDate>
</PubDate>
</JournalIssue>
<Title>Biopolymers</Title>
<ISOAbbreviation>Biopolymers</ISOAbbreviation>
</Journal>
<ArticleTitle>Design, synthesis, and conformational study of biologically active photolabeled analogues of the main immunogenic region of the acetylcholine receptor.</ArticleTitle>
<Pagination><MedlinePgn>37-46</MedlinePgn>
</Pagination>
<Abstract><AbstractText>Photoaffinity labeling is a powerful tool for the characterization of the molecular basis of ligand binding to acceptor molecules, which provides important insights for mapping the bimolecular interfaces. The autoimmune disease myasthenia gravis is caused by autoantibodies against the acetylcholine receptor (AChR). The majority of the anti-AChR antibodies bind to the "main immunogenic region" (MIR) of the AChR. To identify the contact points between the complementarity determining regions of the anti-MIR antibodies that recognize the MIR contact sites of the AChR, we present here three photoreactive dodecapeptide MIR analogues containing the photolabel p-benzoyl-L-phenylalanine (Bpa) moiety, either in position 1 or 11. The structure of the produced 12-mers was analyzed using two-dimensional (1)H-NMR spectroscopy, whereas their binding to anti-MIR monoclonal antibodies (mAbs) was determined by immunochemical assays. In all cases the modifications resulted in conservation of the beta-turn conformation of the N-terminus, which has been proved essential for antibody recognition and increased anti-MIR binding relative to the MIR decapeptide.</AbstractText>
<CopyrightInformation>Copyright 2001 John Wiley & Sons, Inc.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Theodorou</LastName>
<ForeName>V</ForeName>
<Initials>V</Initials>
<AffiliationInfo><Affiliation>Department of Chemistry, University of Ioannina, 45 110 Ioannina, Greece.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Tsikaris</LastName>
<ForeName>V</ForeName>
<Initials>V</Initials>
</Author>
<Author ValidYN="Y"><LastName>Sakarellos-Daitsiotis</LastName>
<ForeName>M</ForeName>
<Initials>M</Initials>
</Author>
<Author ValidYN="Y"><LastName>Avramopoulou</LastName>
<ForeName>V</ForeName>
<Initials>V</Initials>
</Author>
<Author ValidYN="Y"><LastName>Kostelidou</LastName>
<ForeName>K</ForeName>
<Initials>K</Initials>
</Author>
<Author ValidYN="Y"><LastName>Tzartos</LastName>
<ForeName>S J</ForeName>
<Initials>SJ</Initials>
</Author>
<Author ValidYN="Y"><LastName>Sakarellos</LastName>
<ForeName>C</ForeName>
<Initials>C</Initials>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>Biopolymers</MedlineTA>
<NlmUniqueID>0372525</NlmUniqueID>
<ISSNLinking>0006-3525</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D000345">Affinity Labels</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D000911">Antibodies, Monoclonal</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D009842">Oligopeptides</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D010446">Peptide Fragments</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D011978">Receptors, Nicotinic</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000345" MajorTopicYN="N">Affinity Labels</DescriptorName>
<QualifierName UI="Q000138" MajorTopicYN="N">chemical synthesis</QualifierName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000911" MajorTopicYN="N">Antibodies, Monoclonal</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015195" MajorTopicYN="N">Drug Design</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D007120" MajorTopicYN="N">Immunochemistry</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D066298" MajorTopicYN="N">In Vitro Techniques</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009682" MajorTopicYN="N">Magnetic Resonance Spectroscopy</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009842" MajorTopicYN="N">Oligopeptides</DescriptorName>
<QualifierName UI="Q000138" MajorTopicYN="N">chemical synthesis</QualifierName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010446" MajorTopicYN="N">Peptide Fragments</DescriptorName>
<QualifierName UI="Q000138" MajorTopicYN="N">chemical synthesis</QualifierName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010777" MajorTopicYN="N">Photochemistry</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011978" MajorTopicYN="N">Receptors, Nicotinic</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2001</Year>
<Month>10</Month>
<Day>3</Day>
<Hour>10</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2002</Year>
<Month>2</Month>
<Day>28</Day>
<Hour>10</Hour>
<Minute>1</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2001</Year>
<Month>10</Month>
<Day>3</Day>
<Hour>10</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">11582576</ArticleId>
<ArticleId IdType="pii">10.1002/1097-0282(2000)56:1<37::AID-BIP1041>3.0.CO;2-X</ArticleId>
<ArticleId IdType="doi">10.1002/1097-0282(2000)56:1<37::AID-BIP1041>3.0.CO;2-X</ArticleId>
</ArticleIdList>
</PubmedData>
</pubmed>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/MersV1/Data/PubMed/Curation
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002542 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Curation/biblio.hfd -nk 002542 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Sante |area= MersV1 |flux= PubMed |étape= Curation |type= RBID |clé= pubmed:11582576 |texte= Design, synthesis, and conformational study of biologically active photolabeled analogues of the main immunogenic region of the acetylcholine receptor. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Curation/RBID.i -Sk "pubmed:11582576" \ | HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Curation/biblio.hfd \ | NlmPubMed2Wicri -a MersV1
![]() | This area was generated with Dilib version V0.6.33. | ![]() |