Preparation of indium-115-labeled diethylenetriaminetetraacetic acid monoacetamide peptides purified by 8-hydroxyquinoline.
Identifieur interne : 003941 ( Main/Exploration ); précédent : 003940; suivant : 003942Preparation of indium-115-labeled diethylenetriaminetetraacetic acid monoacetamide peptides purified by 8-hydroxyquinoline.
Auteurs : RBID : pubmed:11078578English descriptors
- KwdEn :
- Buffers, Chromatography, High Pressure Liquid, Chromatography, Thin Layer, Indium, Isotope Labeling (methods), Oligopeptides (chemical synthesis), Oligopeptides (isolation & purification), Oxyquinoline (chemistry), Pentetic Acid (chemical synthesis), Pentetic Acid (isolation & purification), Quality Control, Sensitivity and Specificity, Spectrometry, X-Ray Emission, Time Factors.
- MESH :
- chemical , chemical synthesis : Oligopeptides, Pentetic Acid.
- chemical , chemistry : Oxyquinoline.
- chemical , isolation & purification : Oligopeptides, Pentetic Acid.
- chemical : Buffers, Indium.
- methods : Isotope Labeling.
- Chromatography, High Pressure Liquid, Chromatography, Thin Layer, Quality Control, Sensitivity and Specificity, Spectrometry, X-Ray Emission, Time Factors.
Abstract
In this communication we describe a novel procedure for the preparation and purification of diethylenetriaminepentaacetic (DTPA)-acylated and (115)In(3+)-labeled oligopeptides using 8-hydroxyquinoline for the removal and quantification of nonbound indium ions. First the N(alpha)- or N(alpha),N(epsilon)-DTPA oligopeptides containing C-terminal KDEL signal motif were produced by solid-phase synthesis. For this the free carboxyl group of DTPA dianhydride was activated in situ for a short period of time yielding a major product. Reversed-phase HPLC-purified DTPA oligopeptides were labeled with (115)In(3+) in aqueous buffer solution at pH 3.8. For the removal as well as for the detection of uncoordinated (115)In(3+) ions we have utilized the (115)In(3+) complex-forming ability of 8-hydroxyquinoline in chloroform. Following an optimized extraction procedure the free indium ion content was measured by spectrophotometry in the organic phase. Data obtained by this method and verified by total-reflection X-ray fluorescence spectroscopy and thin-layer chromatography demonstrated that free (115)In(3+) could be efficiently removed and sensitively detected in the presence of DTPA oligopeptide chelator. No release of (115)In(3+) from its DTPA complex was observed. This method could be useful for the preparation of indium complexes of peptides and perhaps proteins containing a DTPA moiety and nonradioactive isotope ligand.
DOI: 10.1006/abio.2000.4833
PubMed: 11078578
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Preparation of indium-115-labeled diethylenetriaminetetraacetic acid monoacetamide peptides purified by 8-hydroxyquinoline.</title><author><name sortKey="Nagy, I B" uniqKey="Nagy I">I B Nagy</name><affiliation wicri:level="1"><nlm:affiliation>Research Group for Peptide Chemistry, Hungarian Academy of Sciences, Eötvös L. University, Budapest 112, H-1518, Hungary.</nlm:affiliation><country xml:lang="fr">Hongrie</country><wicri:regionArea>Research Group for Peptide Chemistry, Hungarian Academy of Sciences, Eötvös L. University, Budapest 112, H-1518</wicri:regionArea></affiliation></author><author><name sortKey="Varga, I" uniqKey="Varga I">I Varga</name></author><author><name sortKey="Hudecz, F" uniqKey="Hudecz F">F Hudecz</name></author></titleStmt><publicationStmt><date when="2000">2000</date><idno type="RBID">pubmed:11078578</idno><idno type="pmid">11078578</idno><idno type="doi">10.1006/abio.2000.4833</idno><idno type="wicri:Area/Main/Corpus">003B49</idno><idno type="wicri:Area/Main/Curation">003B49</idno><idno type="wicri:Area/Main/Exploration">003941</idno></publicationStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Buffers</term><term>Chromatography, High Pressure Liquid</term><term>Chromatography, Thin Layer</term><term>Indium</term><term>Isotope Labeling (methods)</term><term>Oligopeptides (chemical synthesis)</term><term>Oligopeptides (isolation & purification)</term><term>Oxyquinoline (chemistry)</term><term>Pentetic Acid (chemical synthesis)</term><term>Pentetic Acid (isolation & purification)</term><term>Quality Control</term><term>Sensitivity and Specificity</term><term>Spectrometry, X-Ray Emission</term><term>Time Factors</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemical synthesis" xml:lang="en"><term>Oligopeptides</term><term>Pentetic Acid</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Oxyquinoline</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Oligopeptides</term><term>Pentetic Acid</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Buffers</term><term>Indium</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Isotope Labeling</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Chromatography, High Pressure Liquid</term><term>Chromatography, Thin Layer</term><term>Quality Control</term><term>Sensitivity and Specificity</term><term>Spectrometry, X-Ray Emission</term><term>Time Factors</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In this communication we describe a novel procedure for the preparation and purification of diethylenetriaminepentaacetic (DTPA)-acylated and (115)In(3+)-labeled oligopeptides using 8-hydroxyquinoline for the removal and quantification of nonbound indium ions. First the N(alpha)- or N(alpha),N(epsilon)-DTPA oligopeptides containing C-terminal KDEL signal motif were produced by solid-phase synthesis. For this the free carboxyl group of DTPA dianhydride was activated in situ for a short period of time yielding a major product. Reversed-phase HPLC-purified DTPA oligopeptides were labeled with (115)In(3+) in aqueous buffer solution at pH 3.8. For the removal as well as for the detection of uncoordinated (115)In(3+) ions we have utilized the (115)In(3+) complex-forming ability of 8-hydroxyquinoline in chloroform. Following an optimized extraction procedure the free indium ion content was measured by spectrophotometry in the organic phase. Data obtained by this method and verified by total-reflection X-ray fluorescence spectroscopy and thin-layer chromatography demonstrated that free (115)In(3+) could be efficiently removed and sensitively detected in the presence of DTPA oligopeptide chelator. No release of (115)In(3+) from its DTPA complex was observed. This method could be useful for the preparation of indium complexes of peptides and perhaps proteins containing a DTPA moiety and nonradioactive isotope ligand.</div></front></TEI><pubmed><MedlineCitation Owner="NLM" Status="MEDLINE"><PMID Version="1">11078578</PMID><DateCreated><Year>2000</Year><Month>12</Month><Day>13</Day></DateCreated><DateCompleted><Year>2001</Year><Month>01</Month><Day>04</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0003-2697</ISSN><JournalIssue CitedMedium="Print"><Volume>287</Volume><Issue>1</Issue><PubDate><Year>2000</Year><Month>Dec</Month><Day>1</Day></PubDate></JournalIssue><Title>Analytical biochemistry</Title><ISOAbbreviation>Anal. Biochem.</ISOAbbreviation></Journal><ArticleTitle>Preparation of indium-115-labeled diethylenetriaminetetraacetic acid monoacetamide peptides purified by 8-hydroxyquinoline.</ArticleTitle><Pagination><MedlinePgn>17-24</MedlinePgn></Pagination><Abstract><AbstractText>In this communication we describe a novel procedure for the preparation and purification of diethylenetriaminepentaacetic (DTPA)-acylated and (115)In(3+)-labeled oligopeptides using 8-hydroxyquinoline for the removal and quantification of nonbound indium ions. First the N(alpha)- or N(alpha),N(epsilon)-DTPA oligopeptides containing C-terminal KDEL signal motif were produced by solid-phase synthesis. For this the free carboxyl group of DTPA dianhydride was activated in situ for a short period of time yielding a major product. Reversed-phase HPLC-purified DTPA oligopeptides were labeled with (115)In(3+) in aqueous buffer solution at pH 3.8. For the removal as well as for the detection of uncoordinated (115)In(3+) ions we have utilized the (115)In(3+) complex-forming ability of 8-hydroxyquinoline in chloroform. Following an optimized extraction procedure the free indium ion content was measured by spectrophotometry in the organic phase. Data obtained by this method and verified by total-reflection X-ray fluorescence spectroscopy and thin-layer chromatography demonstrated that free (115)In(3+) could be efficiently removed and sensitively detected in the presence of DTPA oligopeptide chelator. No release of (115)In(3+) from its DTPA complex was observed. This method could be useful for the preparation of indium complexes of peptides and perhaps proteins containing a DTPA moiety and nonradioactive isotope ligand.</AbstractText><CopyrightInformation>Copyright 2000 Academic Press.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Nagy</LastName><ForeName>I B</ForeName><Initials>IB</Initials><Affiliation>Research Group for Peptide Chemistry, Hungarian Academy of Sciences, Eötvös L. University, Budapest 112, H-1518, Hungary.</Affiliation></Author><Author ValidYN="Y"><LastName>Varga</LastName><ForeName>I</ForeName><Initials>I</Initials></Author><Author ValidYN="Y"><LastName>Hudecz</LastName><ForeName>F</ForeName><Initials>F</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType>Comparative Study</PublicationType><PublicationType>Journal Article</PublicationType><PublicationType>Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>UNITED STATES</Country><MedlineTA>Anal Biochem</MedlineTA><NlmUniqueID>0370535</NlmUniqueID><ISSNLinking>0003-2697</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance>Buffers</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance>Oligopeptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>045A6V3VFX</RegistryNumber><NameOfSubstance>Indium</NameOfSubstance></Chemical><Chemical><RegistryNumber>5UTX5635HP</RegistryNumber><NameOfSubstance>Oxyquinoline</NameOfSubstance></Chemical><Chemical><RegistryNumber>7A314HQM0I</RegistryNumber><NameOfSubstance>Pentetic Acid</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName MajorTopicYN="N">Buffers</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Chromatography, High Pressure Liquid</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Chromatography, Thin Layer</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="Y">Indium</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Isotope Labeling</DescriptorName><QualifierName MajorTopicYN="Y">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Oligopeptides</DescriptorName><QualifierName MajorTopicYN="Y">chemical synthesis</QualifierName><QualifierName MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Oxyquinoline</DescriptorName><QualifierName MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Pentetic Acid</DescriptorName><QualifierName MajorTopicYN="Y">chemical synthesis</QualifierName><QualifierName MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Quality Control</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Sensitivity and Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Spectrometry, X-Ray Emission</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Time Factors</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2000</Year><Month>11</Month><Day>18</Day><Hour>11</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2001</Year><Month>2</Month><Day>28</Day><Hour>10</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2000</Year><Month>11</Month><Day>18</Day><Hour>11</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">11078578</ArticleId><ArticleId IdType="doi">10.1006/abio.2000.4833</ArticleId><ArticleId IdType="pii">S0003-2697(00)94833-4</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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