Design, synthesis, and conformational study of biologically active photolabeled analogues of the main immunogenic region of the acetylcholine receptor.
Identifieur interne : 002542 ( PubMed/Corpus ); 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 ; V. Tsikaris ; M. Sakarellos-Daitsiotis ; V. Avramopoulou ; K. Kostelidou ; S J Tzartos ; C. SakarellosSource :
- Biopolymers [ 0006-3525 ]
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 to Exploration step
pubmed:11582576Le document en format XML
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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. 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Theodorou</name><affiliation><nlm:affiliation>Department of Chemistry, University of Ioannina, 45 110 Ioannina, Greece.</nlm:affiliation></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="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" 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></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, 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