Use of the multipin peptide synthesis technique for the generation of antipeptide sera.
Identifieur interne : 000202 ( Ncbi/Checkpoint ); précédent : 000201; suivant : 000203Use of the multipin peptide synthesis technique for the generation of antipeptide sera.
Auteurs : B. Triantafyllou [Australie] ; G. Tribbick ; N J Maeji ; H M GeysenSource :
- Cell biophysics [ 0163-4992 ]
Descripteurs français
- KwdFr :
- Animaux, Biochimie (), Chromatographie en phase liquide à haute performance, Concentration en ions d'hydrogène, Données de séquences moléculaires, Peptides (), Peptides (analyse), Peptides (immunologie), Similitude de séquences d'acides aminés, Souris, Souris de lignée BALB C, Spécificité des anticorps, Séquence d'acides aminés, Sérums immuns (analyse), Sérums immuns (biosynthèse), Sérums immuns (immunologie), Test ELISA, Épitopes.
- MESH :
- analyse : Peptides, Sérums immuns.
- biosynthèse : Sérums immuns.
- immunologie : Peptides, Sérums immuns.
- Animaux, Biochimie, Chromatographie en phase liquide à haute performance, Concentration en ions d'hydrogène, Données de séquences moléculaires, Peptides, Similitude de séquences d'acides aminés, Souris, Souris de lignée BALB C, Spécificité des anticorps, Séquence d'acides aminés, Test ELISA, Épitopes.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Antibody Specificity, Biochemistry (methods), Chromatography, High Pressure Liquid, Enzyme-Linked Immunosorbent Assay, Epitopes, Hydrogen-Ion Concentration, Immune Sera (analysis), Immune Sera (biosynthesis), Immune Sera (immunology), Mice, Mice, Inbred BALB C, Molecular Sequence Data, Peptides (analysis), Peptides (chemistry), Peptides (immunology), Sequence Homology, Amino Acid.
- MESH :
- chemical , analysis : Immune Sera, Peptides.
- chemical , biosynthesis : Immune Sera.
- chemical , chemistry : Peptides.
- chemical , immunology : Immune Sera, Peptides.
- chemical : Epitopes.
- methods : Biochemistry.
- Amino Acid Sequence, Animals, Antibody Specificity, Chromatography, High Pressure Liquid, Enzyme-Linked Immunosorbent Assay, Hydrogen-Ion Concentration, Mice, Mice, Inbred BALB C, Molecular Sequence Data, Sequence Homology, Amino Acid.
Abstract
The multipin peptide synthesis technique has been used to map antigenic sites of proteins (1,2). Antibodies raised to the whole protein are screened on pin-synthesized overlapping octapeptides homologous with the protein of interest, and the peptides that bind antibodies clearly identify the epitopes. What is described in this study is a method using pin-synthesized peptides to generate specific antibodies to many peptides. Cleavable linkers have been developed (3) that, used together with the multipin peptide synthesis technique, allow the synthesis and cleavage of many thousands of peptides into aqueous solutions at physiological pH. This technique is useful for assays requiring peptides in solution, e.g., mapping of T-cell determinants. A technique has been developed for the cleavage of many peptides from pins and simultaneous coupling to immunogenic carriers (4). The conjugates produced are suitable for the generation of antipeptide antibodies. This procedure is illustrated using several 15 amino acid long peptides (15-mers), homologous with the sequence of a model antigen, myohemerythrin (MHr). The resulting antipeptide sera generated were tested by ELISA for titer and specificity on pin-synthesized peptides and beta-amide peptides and the protein antigen coated to microtiter plates.
DOI: 10.1007/BF02789476
PubMed: 1285329
Affiliations:
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Tribbick</name></author><author><name sortKey="Maeji, N J" sort="Maeji, N J" uniqKey="Maeji N" first="N J" last="Maeji">N J Maeji</name></author><author><name sortKey="Geysen, H M" sort="Geysen, H M" uniqKey="Geysen H" first="H M" last="Geysen">H M Geysen</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="????"><PubDate><MedlineDate>1992 Aug-Dec</MedlineDate></PubDate></date><idno type="RBID">pubmed:1285329</idno><idno type="pmid">1285329</idno><idno type="doi">10.1007/BF02789476</idno><idno type="wicri:Area/PubMed/Corpus">002954</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002954</idno><idno type="wicri:Area/PubMed/Curation">002954</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002954</idno><idno type="wicri:Area/PubMed/Checkpoint">002B17</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">002B17</idno><idno type="wicri:Area/Ncbi/Merge">000202</idno><idno type="wicri:Area/Ncbi/Curation">000202</idno><idno type="wicri:Area/Ncbi/Checkpoint">000202</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Use of the multipin peptide synthesis technique for the generation of antipeptide sera.</title><author><name sortKey="Triantafyllou, B" sort="Triantafyllou, B" uniqKey="Triantafyllou B" first="B" last="Triantafyllou">B. Triantafyllou</name><affiliation wicri:level="1"><nlm:affiliation>Chiron Mimotopes Pty. Ltd., Victoria, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Chiron Mimotopes Pty. Ltd., Victoria</wicri:regionArea><wicri:noRegion>Victoria</wicri:noRegion></affiliation></author><author><name sortKey="Tribbick, G" sort="Tribbick, G" uniqKey="Tribbick G" first="G" last="Tribbick">G. Tribbick</name></author><author><name sortKey="Maeji, N J" sort="Maeji, N J" uniqKey="Maeji N" first="N J" last="Maeji">N J Maeji</name></author><author><name sortKey="Geysen, H M" sort="Geysen, H M" uniqKey="Geysen H" first="H M" last="Geysen">H M Geysen</name></author></analytic><series><title level="j">Cell biophysics</title><idno type="ISSN">0163-4992</idno></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Antibody Specificity</term><term>Biochemistry (methods)</term><term>Chromatography, High Pressure Liquid</term><term>Enzyme-Linked Immunosorbent Assay</term><term>Epitopes</term><term>Hydrogen-Ion Concentration</term><term>Immune Sera (analysis)</term><term>Immune Sera (biosynthesis)</term><term>Immune Sera (immunology)</term><term>Mice</term><term>Mice, Inbred BALB C</term><term>Molecular Sequence Data</term><term>Peptides (analysis)</term><term>Peptides (chemistry)</term><term>Peptides (immunology)</term><term>Sequence Homology, Amino Acid</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Biochimie ()</term><term>Chromatographie en phase liquide à haute performance</term><term>Concentration en ions d'hydrogène</term><term>Données de séquences moléculaires</term><term>Peptides ()</term><term>Peptides (analyse)</term><term>Peptides (immunologie)</term><term>Similitude de séquences d'acides aminés</term><term>Souris</term><term>Souris de lignée BALB C</term><term>Spécificité des anticorps</term><term>Séquence d'acides aminés</term><term>Sérums immuns (analyse)</term><term>Sérums immuns (biosynthèse)</term><term>Sérums immuns (immunologie)</term><term>Test ELISA</term><term>Épitopes</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Immune Sera</term><term>Peptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Immune Sera</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Peptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Immune Sera</term><term>Peptides</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Epitopes</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Peptides</term><term>Sérums immuns</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Sérums immuns</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Peptides</term><term>Sérums immuns</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Biochemistry</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Antibody Specificity</term><term>Chromatography, High Pressure Liquid</term><term>Enzyme-Linked Immunosorbent Assay</term><term>Hydrogen-Ion Concentration</term><term>Mice</term><term>Mice, Inbred BALB C</term><term>Molecular Sequence Data</term><term>Sequence Homology, Amino Acid</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Biochimie</term><term>Chromatographie en phase liquide à haute performance</term><term>Concentration en ions d'hydrogène</term><term>Données de séquences moléculaires</term><term>Peptides</term><term>Similitude de séquences d'acides aminés</term><term>Souris</term><term>Souris de lignée BALB C</term><term>Spécificité des anticorps</term><term>Séquence d'acides aminés</term><term>Test ELISA</term><term>Épitopes</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The multipin peptide synthesis technique has been used to map antigenic sites of proteins (1,2). Antibodies raised to the whole protein are screened on pin-synthesized overlapping octapeptides homologous with the protein of interest, and the peptides that bind antibodies clearly identify the epitopes. What is described in this study is a method using pin-synthesized peptides to generate specific antibodies to many peptides. Cleavable linkers have been developed (3) that, used together with the multipin peptide synthesis technique, allow the synthesis and cleavage of many thousands of peptides into aqueous solutions at physiological pH. This technique is useful for assays requiring peptides in solution, e.g., mapping of T-cell determinants. A technique has been developed for the cleavage of many peptides from pins and simultaneous coupling to immunogenic carriers (4). The conjugates produced are suitable for the generation of antipeptide antibodies. This procedure is illustrated using several 15 amino acid long peptides (15-mers), homologous with the sequence of a model antigen, myohemerythrin (MHr). The resulting antipeptide sera generated were tested by ELISA for titer and specificity on pin-synthesized peptides and beta-amide peptides and the protein antigen coated to microtiter plates.</div></front></TEI><affiliations><list><country><li>Australie</li></country></list><tree><noCountry><name sortKey="Geysen, H M" sort="Geysen, H M" uniqKey="Geysen H" first="H M" last="Geysen">H M Geysen</name><name sortKey="Maeji, N J" sort="Maeji, N J" uniqKey="Maeji N" first="N J" last="Maeji">N J Maeji</name><name sortKey="Tribbick, G" sort="Tribbick, G" uniqKey="Tribbick G" first="G" last="Tribbick">G. Tribbick</name></noCountry><country name="Australie"><noRegion><name sortKey="Triantafyllou, B" sort="Triantafyllou, B" uniqKey="Triantafyllou B" first="B" last="Triantafyllou">B. 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