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Identification, affinity characterisation and biological interactions of lectin-like peptide-carbohydrate complexes derived from human TNF-alpha using high-resolution mass spectrometry

Identification, affinity characterisation and biological interactions of lectin-like peptide-carbohydrate complexes derived from human TNF-alpha using high-resolution mass spectrometry

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MARQUARDT, Andreas, Bogdan BERNEVIC, Michael PRZYBYLSKI, 2007. Identification, affinity characterisation and biological interactions of lectin-like peptide-carbohydrate complexes derived from human TNF-alpha using high-resolution mass spectrometry. In: Journal of Peptide Science. 13(12), pp. 803-810. ISSN 1075-2617. eISSN 1099-1387

@article{Marquardt2007Ident-1044, title={Identification, affinity characterisation and biological interactions of lectin-like peptide-carbohydrate complexes derived from human TNF-alpha using high-resolution mass spectrometry}, year={2007}, doi={10.1002/psc.902}, number={12}, volume={13}, issn={1075-2617}, journal={Journal of Peptide Science}, pages={803--810}, author={Marquardt, Andreas and Bernevic, Bogdan 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/123456789/1044"> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-22T17:54:56Z</dcterms:available> <dc:creator>Przybylski, Michael</dc:creator> <dcterms:abstract xml:lang="eng">A cyclic disulfide heptadecapeptide (TIP17ox; 2) derived from the lectin-like 17-amino acid domain of human tumor necrosis factor-α [TNF-α (100-116)] was synthesised and demonstrated to bind specifically to N,N-diacetylchitobiose, a disaccharide present in many glycan structures of glycoproteins. Although the TIP domain forms a loop structure in the native TNF-α protein, we show in this study by high-resolution ESI-FTICR mass spectrometry that a homologous linear heptadecapeptide (TIP17rd; 1) binds with comparable affinity to chitobiose, suggesting that cyclisation is not essential for carbohydrate binding. ESI-FTICR-MS was used as an efficient tool for the direct molecular characterisation of TIP peptide-carbohydrate complexes. The specific binding of the TNF-TIP domain to chitobiose and other carbohydrate motifs in glycoproteins may explain the high proteolytic stability of these peptides in biological fluids. A considerably higher proteolytic stability in human plasma was found by mass spectrometric analysis for the cyclic TIP peptide 2, compared to the linear peptide 1. Furthermore, affinity-proteomics studies using immobilised cyclic TIP peptide 2 provided the identification of specific interacting glycoproteins in plasma.</dcterms:abstract> <dcterms:rights rdf:resource="https://creativecommons.org/licenses/by-nc-nd/2.0/legalcode"/> <dc:contributor>Marquardt, Andreas</dc:contributor> <dc:rights>deposit-license</dc:rights> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-22T17:54:56Z</dc:date> <dc:creator>Marquardt, Andreas</dc:creator> <dcterms:issued>2007</dcterms:issued> <dcterms:title>Identification, affinity characterisation and biological interactions of lectin-like peptide-carbohydrate complexes derived from human TNF-alpha using high-resolution mass spectrometry</dcterms:title> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/1044"/> <dcterms:bibliographicCitation>First publ. in: Journal of Peptide Science 13 (2007), 12, pp. 803-810</dcterms:bibliographicCitation> <dc:creator>Bernevic, Bogdan</dc:creator> <dc:contributor>Bernevic, Bogdan</dc:contributor> <dc:contributor>Przybylski, Michael</dc:contributor> <dc:language>eng</dc:language> </rdf:Description> </rdf:RDF>

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