Publikation: Synthetic Approaches to Study Multivalent Carbohydrate Lectin Interactions
Dateien
Datum
Autor:innen
Herausgeber:innen
ISSN der Zeitschrift
Electronic ISSN
ISBN
Bibliografische Daten
Verlag
Schriftenreihe
Auflagebezeichnung
URI (zitierfähiger Link)
Internationale Patentnummer
Link zur Lizenz
Angaben zur Forschungsförderung
Projekt
Open Access-Veröffentlichung
Sammlungen
Core Facility der Universität Konstanz
Titel in einer weiteren Sprache
Publikationstyp
Publikationsstatus
Erschienen in
Zusammenfassung
The specific recognition of carbohydrate structures in biological systems by carbohydrate-binding proteins (lectins) is the basis of numerous intra- and intercellular events ranging from the control of protein folding to cell cell communication during development, inflammation, and cancer metastasis. Investigation of carbohydrate lectin interactions can be approached from two directions. One is characterization of the protein part by molecular biology and structure determination (X-ray crystallography, NMR spectroscopy). In the other approach, which relies on synthetic organic chemistry, the specificity and affinity of modified or artificial lectin ligands and their effect on lectin function is studied. High-affinity lectin ligands are, furthermore, of considerable medicinal interest in the diagnosis and inhibition of carbohydrate-mediated processes such as inflammation or microbial adhesion. The generation of high-affinity lectin ligands, however, is not trivial because most saccharide ligands bind to their protein receptors only weakly with dissociation constants typically in the milli- to micromolar range. Because many lectins have several binding sites or occur in oligomeric or clustered form on cell membranes, the creation of multivalent carbohydrate derivatives is a promising means of producing high-affinity ligands.
Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
Schlagwörter
Konferenz
Rezension
Zitieren
ISO 690
WITTMANN, Valentin, 2004. Synthetic Approaches to Study Multivalent Carbohydrate Lectin Interactions. In: SCHMUCK, Carsten, ed.. Highlights in Bioorganic Chemistry. Weinheim: Wiley, 2004, pp. 203-213BibTex
@incollection{Wittmann2004Synth-9980, year={2004}, title={Synthetic Approaches to Study Multivalent Carbohydrate Lectin Interactions}, publisher={Wiley}, address={Weinheim}, booktitle={Highlights in Bioorganic Chemistry}, pages={203--213}, editor={Schmuck, Carsten}, author={Wittmann, Valentin} }
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/123456789/9980"> <foaf:homepage rdf:resource="http://localhost:8080/"/> <dcterms:rights rdf:resource="http://creativecommons.org/licenses/by-nc-nd/2.0/"/> <dcterms:bibliographicCitation>First publ. in: Highlights in Bioorganic Chemistry / Carsten Schmuck (ed.). - Weinheim: Wiley, 2004, pp. 203-213</dcterms:bibliographicCitation> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/9980"/> <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/9980/1/witt_032a.pdf"/> <dcterms:abstract xml:lang="eng">The specific recognition of carbohydrate structures in biological systems by carbohydrate-binding proteins (lectins) is the basis of numerous intra- and intercellular events ranging from the control of protein folding to cell cell communication during development, inflammation, and cancer metastasis. Investigation of carbohydrate lectin interactions can be approached from two directions. One is characterization of the protein part by molecular biology and structure determination (X-ray crystallography, NMR spectroscopy). In the other approach, which relies on synthetic organic chemistry, the specificity and affinity of modified or artificial lectin ligands and their effect on lectin function is studied. High-affinity lectin ligands are, furthermore, of considerable medicinal interest in the diagnosis and inhibition of carbohydrate-mediated processes such as inflammation or microbial adhesion. The generation of high-affinity lectin ligands, however, is not trivial because most saccharide ligands bind to their protein receptors only weakly with dissociation constants typically in the milli- to micromolar range. Because many lectins have several binding sites or occur in oligomeric or clustered form on cell membranes, the creation of multivalent carbohydrate derivatives is a promising means of producing high-affinity ligands.</dcterms:abstract> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T18:15:43Z</dcterms:available> <dc:contributor>Wittmann, Valentin</dc:contributor> <dc:format>application/pdf</dc:format> <dcterms:title>Synthetic Approaches to Study Multivalent Carbohydrate Lectin Interactions</dcterms:title> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dc:creator>Wittmann, Valentin</dc:creator> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T18:15:43Z</dc:date> <dc:rights>Attribution-NonCommercial-NoDerivs 2.0 Generic</dc:rights> <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/> <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/9980/1/witt_032a.pdf"/> <dcterms:issued>2004</dcterms:issued> <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/> <dc:language>eng</dc:language> </rdf:Description> </rdf:RDF>