@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}
}

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    <dc:creator>Manea, Marilena</dc:creator>
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    <dc:contributor>Przybylski, Michael</dc:contributor>
    <dc:contributor>Bösze, Szilvia</dc:contributor>
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    <dc:contributor>Mezö, Gábor</dc:contributor>
    <dc:contributor>Jakab, Annamária</dc:contributor>
    <dcterms:issued>2004-12</dcterms:issued>
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    <dc:creator>Jakab, Annamária</dc:creator>
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    <dc:creator>Mezö, Gábor</dc:creator>
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    <dc:contributor>Schlosser, Gitta</dc:contributor>
    <dc:creator>Schlosser, Gitta</dc:creator>
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    <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>
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    <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>
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