Synthesis and structural characterization of bioactive peptide conjugates using thioether linkage approaches

Mezö, Gábor; Manea, Marilena; Jakab, Annamária; Kapuvári, Bence; Bösze, Szilvia; Schlosser, Gitta; Przybylski, Michael; Hudecz, Ferenc

Synthesis and structural characterization of bioactive peptide conjugates using thioether linkage approaches

Dateien

Zu diesem Dokument gibt es keine Dateien.

Datum

2004

Autor:innen

Mezö, Gábor

Manea, Marilena

Jakab, Annamária

Kapuvári, Bence

Bösze, Szilvia

Schlosser, Gitta

Przybylski, Michael

Hudecz, Ferenc

Publikationstyp

Zeitschriftenartikel

Publikationsstatus

Published

Erschienen in

Journal of Peptide Science. 2004, 10(12), pp. 701-713. ISSN 1075-2617. Available under: doi: 10.1002/psc.583

Zusammenfassung

Applications of cysteine-insertion and thioether linkage approaches to the preparation of a number of bioactive peptide conjugates are reported. Peptides containing epitopes from (i) herpes simplex virus type 1 glycoprotein D, (ii) a specific N-terminal beta-amyloid epitope recognized by therapeutically active antibodies, and (iii) a GnRH-III peptide from sea lamprey with antitumour activity, were elongated with Cys residues and attached to a chloroacetylated tetratuftsin derivative carrier via a thioether linkage either directly, or by insertion of a spacer. The structures and molecular homogeneity of all the peptide conjugates were ascertained by HPLC, MALDI and electrospray mass spectrometry. The use of a spacer such as an oligoglycine or GFLG-tetrapeptide gave an increased yield in the conjugation reaction and enhanced reaction rates. In the formation of cysteinyl-thioether linkages, it was found that the position of flanking Cys residues markedly influenced the conjugation reaction and the formation of intermolecular epitope disulfide-dimers. C-terminal Cys residues gave thioether conjugates with significantly diminished epitope-dimerization, while Cys at the N-terminal caused rapid disulfide-dimerization, thereby preventing efficient conjugation.

Fachgebiet (DDC)

540 Chemie

Schlagwörter

peptide conjugates, tetratuftsin derivative, thioether bond, Cys-peptides, HSV epitope peptide, β-amyloid epitope, GnRH-II

Zitieren

ISO 690

MEZÖ, Gábor, Marilena MANEA, Annamária JAKAB, Bence KAPUVÁRI, Szilvia BÖSZE, Gitta SCHLOSSER, Michael PRZYBYLSKI, Ferenc HUDECZ, 2004. Synthesis and structural characterization of bioactive peptide conjugates using thioether linkage approaches. In: Journal of Peptide Science. 2004, 10(12), pp. 701-713. ISSN 1075-2617. Available under: doi: 10.1002/psc.583

BibTex

@article{Mezo2004-12Synth-17580,
  year={2004},
  doi={10.1002/psc.583},
  title={Synthesis and structural characterization of bioactive peptide conjugates using thioether linkage approaches},
  number={12},
  volume={10},
  issn={1075-2617},
  journal={Journal of Peptide Science},
  pages={701--713},
  author={Mezö, Gábor and Manea, Marilena and Jakab, Annamária and Kapuvári, Bence and Bösze, Szilvia and Schlosser, Gitta and Przybylski, Michael and Hudecz, Ferenc}
}

RDF

<rdf:RDF
    xmlns:dcterms="http://purl.org/dc/terms/"
    xmlns:dc="http://purl.org/dc/elements/1.1/"
    xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#"
    xmlns:bibo="http://purl.org/ontology/bibo/"
    xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#"
    xmlns:foaf="http://xmlns.com/foaf/0.1/"
    xmlns:void="http://rdfs.org/ns/void#"
    xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > 
  <rdf:Description rdf:about="https://kops.uni-konstanz.de/server/rdf/resource/123456789/17580">
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/52"/>
    <dc:creator>Manea, Marilena</dc:creator>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/17580"/>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dc:contributor>Przybylski, Michael</dc:contributor>
    <dc:contributor>Bösze, Szilvia</dc:contributor>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/52"/>
    <dc:contributor>Mezö, Gábor</dc:contributor>
    <dc:contributor>Jakab, Annamária</dc:contributor>
    <dcterms:issued>2004-12</dcterms:issued>
    <dc:rights>terms-of-use</dc:rights>
    <dc:creator>Jakab, Annamária</dc:creator>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/>
    <dc:creator>Mezö, Gábor</dc:creator>
    <dc:contributor>Hudecz, Ferenc</dc:contributor>
    <dc:contributor>Schlosser, Gitta</dc:contributor>
    <dc:creator>Schlosser, Gitta</dc:creator>
    <dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/>
    <dcterms:title>Synthesis and structural characterization of bioactive peptide conjugates using thioether linkage approaches</dcterms:title>
    <dcterms:bibliographicCitation>Publ. in: Journal of peptide science ; 10 (2004), 12. - S. 701-713</dcterms:bibliographicCitation>
    <dc:contributor>Kapuvári, Bence</dc:contributor>
    <dc:creator>Kapuvári, Bence</dc:creator>
    <dc:creator>Bösze, Szilvia</dc:creator>
    <dc:creator>Przybylski, Michael</dc:creator>
    <dc:creator>Hudecz, Ferenc</dc:creator>
    <dc:language>eng</dc:language>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-01-13T07:31:13Z</dc:date>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-01-13T07:31:13Z</dcterms:available>
    <dcterms:abstract xml:lang="eng">Applications of cysteine-insertion and thioether linkage approaches to the preparation of a number of bioactive peptide conjugates are reported. Peptides containing epitopes from (i) herpes simplex virus type 1 glycoprotein D, (ii) a specific N-terminal beta-amyloid epitope recognized by therapeutically active antibodies, and (iii) a GnRH-III peptide from sea lamprey with antitumour activity, were elongated with Cys residues and attached to a chloroacetylated tetratuftsin derivative carrier via a thioether linkage either directly, or by insertion of a spacer. The structures and molecular homogeneity of all the peptide conjugates were ascertained by HPLC, MALDI and electrospray mass spectrometry. The use of a spacer such as an oligoglycine or GFLG-tetrapeptide gave an increased yield in the conjugation reaction and enhanced reaction rates. In the formation of cysteinyl-thioether linkages, it was found that the position of flanking Cys residues markedly influenced the conjugation reaction and the formation of intermolecular epitope disulfide-dimers. C-terminal Cys residues gave thioether conjugates with significantly diminished epitope-dimerization, while Cys at the N-terminal caused rapid disulfide-dimerization, thereby preventing efficient conjugation.</dcterms:abstract>
    <dc:contributor>Manea, Marilena</dc:contributor>
  </rdf:Description>
</rdf:RDF>

Universitätsbibliographie

Ja