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Functional Ubiquitin Conjugates with Lysine-epsilon-Amino-Specific Linkage by Thioether Ligation of Cysteinyl-Ubiquitin Peptide Building Blocks

Functional Ubiquitin Conjugates with Lysine-epsilon-Amino-Specific Linkage by Thioether Ligation of Cysteinyl-Ubiquitin Peptide Building Blocks

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JUNG, Ji Eun, Hans-Peter WOLLSCHEID, Andreas MARQUARDT, Marilena MANEA, Martin SCHEFFNER, Michael PRZYBYLSKI, 2009. Functional Ubiquitin Conjugates with Lysine-epsilon-Amino-Specific Linkage by Thioether Ligation of Cysteinyl-Ubiquitin Peptide Building Blocks. In: Bioconjugate Chemistry. 20(6), pp. 1152-1162

@article{Jung2009Funct-3287, title={Functional Ubiquitin Conjugates with Lysine-epsilon-Amino-Specific Linkage by Thioether Ligation of Cysteinyl-Ubiquitin Peptide Building Blocks}, year={2009}, doi={10.1021/bc800539p}, number={6}, volume={20}, journal={Bioconjugate Chemistry}, pages={1152--1162}, author={Jung, Ji Eun and Wollscheid, Hans-Peter and Marquardt, Andreas and Manea, Marilena and Scheffner, Martin and Przybylski, Michael} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/3287"> <dc:contributor>Jung, Ji Eun</dc:contributor> <dc:creator>Jung, Ji Eun</dc:creator> <dc:contributor>Marquardt, Andreas</dc:contributor> <dc:contributor>Wollscheid, Hans-Peter</dc:contributor> <dc:creator>Scheffner, Martin</dc:creator> <dc:creator>Manea, Marilena</dc:creator> <dc:contributor>Manea, Marilena</dc:contributor> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-23T10:19:52Z</dc:date> <dc:contributor>Scheffner, Martin</dc:contributor> <dc:creator>Przybylski, Michael</dc:creator> <dc:creator>Wollscheid, Hans-Peter</dc:creator> <dcterms:issued>2009</dcterms:issued> <dc:creator>Marquardt, Andreas</dc:creator> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-23T10:19:52Z</dcterms:available> <dcterms:rights rdf:resource="http://nbn-resolving.org/urn:nbn:de:bsz:352-20140905103416863-3868037-7"/> <dc:language>eng</dc:language> <dc:contributor>Przybylski, Michael</dc:contributor> <dcterms:abstract xml:lang="deu">The modification of ubiquitin to defined oligo-ubiquitinated conjugates has received considerable interest due to the finding that isomeric oligo-ubiquitin conjugates exhibit distinct differences in their biochemical functions, depending on the specific lysine-ε-amino linkage used for conjugate formation. Here, we report the design and development of a thioether linkage-based approach for the synthesis of oligo-ubiquitin conjugates with lysine-specific branching by thioether ligation of a linear ubiquitin peptide containing a C-terminal cysteine residue as the "donor" component, with a corresponding lysine-ε-amino-branched haloacyl-activated ubiquitin "acceptor" peptide. This approach was successfully used for the synthesis of a lysine-63-linked diubiquitin conjugate by ligation of the modified ubiquitin(1-52)-Cys- donor peptide to the N-terminal Arg-54 residue of the branched Lys-63-linked acceptor peptide, ubiquitin(54-76)2. Advantages of the present approach are as follows: (i) the conjugation reaction is performed in solution using suitable preformed donor ubiquitin peptides with a C-terminal Cys residue, and (ii) different corresponding N-chloroacetylated ubiquitin acceptor peptides containing the branched Lys residue are employed, providing broad applicability to the preparation of isomeric oligo-ubiquitin conjugates. The Lys-63-diubiquitin conjugate 7 described here was purified by semipreparative HPLC, and its structure and homogeneity ascertained by HPLC and high-resolution MALDI and electrospray-mass spectrometry. CD spectra and molecular modeling indicate a conformationally stable structure of the conjugate with spatial separation of the ubiquitin parts of the Lys-63 linkage. Moreover, the activity of the thioether-linked diubiquitin conjugate was ascertained by in vitro autoubiquitination assay. These results indicate the feasibility of this approach for the preparation of functional oligo-ubiquitin conjugates.</dcterms:abstract> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/3287"/> <dcterms:title>Functional Ubiquitin Conjugates with Lysine-epsilon-Amino-Specific Linkage by Thioether Ligation of Cysteinyl-Ubiquitin Peptide Building Blocks</dcterms:title> <dcterms:bibliographicCitation>Publ. in: Bioconjugate Chemistry 20 (2009), 6, pp. 1152-1162</dcterms:bibliographicCitation> <dc:rights>deposit-license</dc:rights> </rdf:Description> </rdf:RDF>

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