Structure of antibody-bound peptides and retro-inverso analogues. A transferred nuclear Overhauser effect spectroscopy and molecular dynamics approach.
Identifieur interne : 000225 ( PubMed/Corpus ); précédent : 000224; suivant : 000226Structure of antibody-bound peptides and retro-inverso analogues. A transferred nuclear Overhauser effect spectroscopy and molecular dynamics approach.
Auteurs : A. Phan-Chan-Du ; M C Petit ; G. Guichard ; J P Briand ; S. Muller ; M T CungSource :
- Biochemistry [ 0006-2960 ] ; 2001.
English descriptors
- KwdEn :
- Antibodies, Monoclonal (metabolism), Antibody Affinity, Binding Sites, Antibody, Cross Reactions, Energy Transfer, Histones (chemical synthesis), Histones (immunology), Histones (metabolism), Kinetics, Ligands, Nuclear Magnetic Resonance, Biomolecular, Oligopeptides (chemical synthesis), Oligopeptides (immunology), Oligopeptides (metabolism), Protein Conformation, Protein Structure, Secondary, Protons, Stereoisomerism, Surface Plasmon Resonance.
- MESH :
- chemical , chemical synthesis : Histones, Oligopeptides.
- chemical , immunology : Histones, Oligopeptides.
- chemical , metabolism : Antibodies, Monoclonal, Histones, Oligopeptides.
- Antibody Affinity, Binding Sites, Antibody, Cross Reactions, Energy Transfer, Kinetics, Ligands, Nuclear Magnetic Resonance, Biomolecular, Protein Conformation, Protein Structure, Secondary, Protons, Stereoisomerism, Surface Plasmon Resonance.
Abstract
The three-dimensional structures of the two L-peptides, H-CGGIRGERA-OH, called L(A), and H-CGGIRGERG-OH, called L(G), corresponding or close to the IRGERA sequence present in the C-terminal region (residues 130-135) of histone H3, and their retro-inverso analogues HO-mAreGriGGC-NH2, called RI(mA), and HO-mGreGriGGC-NH2, called RI(mG), have been studied by two-dimensional 1H NMR and molecular dynamics calculations in association with a monoclonal antibody generated against L(A). At 25 degrees C, the affinity constants of the monoclonal antibody with respect to RI(mA) and RI(mG) were 75- and 270-fold higher than those measured with the homologous L(A) and L(G) peptides, respectively. Due to the spontaneous epimerization of the mA malonic residue, RI(mA) gave rise to two sets of resonances. With regard to the NH amide region, one set was similar to that for RI(mG) while the second was similar to those for the parent L-peptides L(A) and L(G). The antibody-bound conformations of the two couples of L- and retro-inverso peptides have been analyzed using molecular modeling calculations based on the transferred NOE interproton distances. Folded structures appeared in both cases with a type II' beta-turn in the parent GGIR sequence and a type I' beta-turn in the retro-inverso reGr sequence.
PubMed: 11341837
Links to Exploration step
pubmed:11341837Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Structure of antibody-bound peptides and retro-inverso analogues. A transferred nuclear Overhauser effect spectroscopy and molecular dynamics approach.</title><author><name sortKey="Phan Chan Du, A" sort="Phan Chan Du, A" uniqKey="Phan Chan Du A" first="A" last="Phan-Chan-Du">A. Phan-Chan-Du</name><affiliation><nlm:affiliation>Laboratoire de Chimie-Physique Macromoléculaire, UMR 7568 CNRS-INPL, Groupe ENSIC, 1 rue Grandville, B.P. 451, 54001 Nancy Cedex, France.</nlm:affiliation></affiliation></author><author><name sortKey="Petit, M C" sort="Petit, M C" uniqKey="Petit M" first="M C" last="Petit">M C Petit</name></author><author><name sortKey="Guichard, G" sort="Guichard, G" uniqKey="Guichard G" first="G" last="Guichard">G. Guichard</name></author><author><name sortKey="Briand, J P" sort="Briand, J P" uniqKey="Briand J" first="J P" last="Briand">J P Briand</name></author><author><name sortKey="Muller, S" sort="Muller, S" uniqKey="Muller S" first="S" last="Muller">S. Muller</name></author><author><name sortKey="Cung, M T" sort="Cung, M T" uniqKey="Cung M" first="M T" last="Cung">M T Cung</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2001">2001</date><idno type="RBID">pubmed:11341837</idno><idno type="pmid">11341837</idno><idno type="wicri:Area/PubMed/Corpus">000225</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000225</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Structure of antibody-bound peptides and retro-inverso analogues. A transferred nuclear Overhauser effect spectroscopy and molecular dynamics approach.</title><author><name sortKey="Phan Chan Du, A" sort="Phan Chan Du, A" uniqKey="Phan Chan Du A" first="A" last="Phan-Chan-Du">A. Phan-Chan-Du</name><affiliation><nlm:affiliation>Laboratoire de Chimie-Physique Macromoléculaire, UMR 7568 CNRS-INPL, Groupe ENSIC, 1 rue Grandville, B.P. 451, 54001 Nancy Cedex, France.</nlm:affiliation></affiliation></author><author><name sortKey="Petit, M C" sort="Petit, M C" uniqKey="Petit M" first="M C" last="Petit">M C Petit</name></author><author><name sortKey="Guichard, G" sort="Guichard, G" uniqKey="Guichard G" first="G" last="Guichard">G. Guichard</name></author><author><name sortKey="Briand, J P" sort="Briand, J P" uniqKey="Briand J" first="J P" last="Briand">J P Briand</name></author><author><name sortKey="Muller, S" sort="Muller, S" uniqKey="Muller S" first="S" last="Muller">S. Muller</name></author><author><name sortKey="Cung, M T" sort="Cung, M T" uniqKey="Cung M" first="M T" last="Cung">M T Cung</name></author></analytic><series><title level="j">Biochemistry</title><idno type="ISSN">0006-2960</idno><imprint><date when="2001" type="published">2001</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antibodies, Monoclonal (metabolism)</term><term>Antibody Affinity</term><term>Binding Sites, Antibody</term><term>Cross Reactions</term><term>Energy Transfer</term><term>Histones (chemical synthesis)</term><term>Histones (immunology)</term><term>Histones (metabolism)</term><term>Kinetics</term><term>Ligands</term><term>Nuclear Magnetic Resonance, Biomolecular</term><term>Oligopeptides (chemical synthesis)</term><term>Oligopeptides (immunology)</term><term>Oligopeptides (metabolism)</term><term>Protein Conformation</term><term>Protein Structure, Secondary</term><term>Protons</term><term>Stereoisomerism</term><term>Surface Plasmon Resonance</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemical synthesis" xml:lang="en"><term>Histones</term><term>Oligopeptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Histones</term><term>Oligopeptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Antibodies, Monoclonal</term><term>Histones</term><term>Oligopeptides</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Antibody Affinity</term><term>Binding Sites, Antibody</term><term>Cross Reactions</term><term>Energy Transfer</term><term>Kinetics</term><term>Ligands</term><term>Nuclear Magnetic Resonance, Biomolecular</term><term>Protein Conformation</term><term>Protein Structure, Secondary</term><term>Protons</term><term>Stereoisomerism</term><term>Surface Plasmon Resonance</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The three-dimensional structures of the two L-peptides, H-CGGIRGERA-OH, called L(A), and H-CGGIRGERG-OH, called L(G), corresponding or close to the IRGERA sequence present in the C-terminal region (residues 130-135) of histone H3, and their retro-inverso analogues HO-mAreGriGGC-NH2, called RI(mA), and HO-mGreGriGGC-NH2, called RI(mG), have been studied by two-dimensional 1H NMR and molecular dynamics calculations in association with a monoclonal antibody generated against L(A). At 25 degrees C, the affinity constants of the monoclonal antibody with respect to RI(mA) and RI(mG) were 75- and 270-fold higher than those measured with the homologous L(A) and L(G) peptides, respectively. Due to the spontaneous epimerization of the mA malonic residue, RI(mA) gave rise to two sets of resonances. With regard to the NH amide region, one set was similar to that for RI(mG) while the second was similar to those for the parent L-peptides L(A) and L(G). The antibody-bound conformations of the two couples of L- and retro-inverso peptides have been analyzed using molecular modeling calculations based on the transferred NOE interproton distances. Folded structures appeared in both cases with a type II' beta-turn in the parent GGIR sequence and a type I' beta-turn in the retro-inverso reGr sequence.</div></front></TEI><pubmed><MedlineCitation Owner="NLM" Status="MEDLINE"><PMID Version="1">11341837</PMID><DateCreated><Year>2001</Year><Month>05</Month><Day>08</Day></DateCreated><DateCompleted><Year>2001</Year><Month>08</Month><Day>02</Day></DateCompleted><DateRevised><Year>2011</Year><Month>11</Month><Day>17</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-2960</ISSN><JournalIssue CitedMedium="Print"><Volume>40</Volume><Issue>19</Issue><PubDate><Year>2001</Year><Month>May</Month><Day>15</Day></PubDate></JournalIssue><Title>Biochemistry</Title><ISOAbbreviation>Biochemistry</ISOAbbreviation></Journal><ArticleTitle>Structure of antibody-bound peptides and retro-inverso analogues. A transferred nuclear Overhauser effect spectroscopy and molecular dynamics approach.</ArticleTitle><Pagination><MedlinePgn>5720-7</MedlinePgn></Pagination><Abstract><AbstractText>The three-dimensional structures of the two L-peptides, H-CGGIRGERA-OH, called L(A), and H-CGGIRGERG-OH, called L(G), corresponding or close to the IRGERA sequence present in the C-terminal region (residues 130-135) of histone H3, and their retro-inverso analogues HO-mAreGriGGC-NH2, called RI(mA), and HO-mGreGriGGC-NH2, called RI(mG), have been studied by two-dimensional 1H NMR and molecular dynamics calculations in association with a monoclonal antibody generated against L(A). At 25 degrees C, the affinity constants of the monoclonal antibody with respect to RI(mA) and RI(mG) were 75- and 270-fold higher than those measured with the homologous L(A) and L(G) peptides, respectively. Due to the spontaneous epimerization of the mA malonic residue, RI(mA) gave rise to two sets of resonances. With regard to the NH amide region, one set was similar to that for RI(mG) while the second was similar to those for the parent L-peptides L(A) and L(G). The antibody-bound conformations of the two couples of L- and retro-inverso peptides have been analyzed using molecular modeling calculations based on the transferred NOE interproton distances. Folded structures appeared in both cases with a type II' beta-turn in the parent GGIR sequence and a type I' beta-turn in the retro-inverso reGr sequence.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Phan-Chan-Du</LastName><ForeName>A</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Laboratoire de Chimie-Physique Macromoléculaire, UMR 7568 CNRS-INPL, Groupe ENSIC, 1 rue Grandville, B.P. 451, 54001 Nancy Cedex, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Petit</LastName><ForeName>M C</ForeName><Initials>MC</Initials></Author><Author ValidYN="Y"><LastName>Guichard</LastName><ForeName>G</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Briand</LastName><ForeName>J P</ForeName><Initials>JP</Initials></Author><Author ValidYN="Y"><LastName>Muller</LastName><ForeName>S</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Cung</LastName><ForeName>M 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MajorTopicYN="N" UI="D004735">Energy Transfer</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D006657">Histones</DescriptorName><QualifierName MajorTopicYN="N" UI="Q000138">chemical synthesis</QualifierName><QualifierName MajorTopicYN="Y" UI="Q000276">immunology</QualifierName><QualifierName MajorTopicYN="Y" UI="Q000378">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D007700">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D008024">Ligands</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D019906">Nuclear Magnetic Resonance, Biomolecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D009842">Oligopeptides</DescriptorName><QualifierName MajorTopicYN="N" UI="Q000138">chemical synthesis</QualifierName><QualifierName MajorTopicYN="Y" UI="Q000276">immunology</QualifierName><QualifierName MajorTopicYN="Y" 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