@article{Andre2009Carba-9877,
  year={2009},
  doi={10.1021/bc900152w},
  title={Carbamate-Linked Lactose : Design of Clusters and Evidence for Selectivity to Block Binding of Human Lectins to (Neo)Glycoproteins with Increasing Degree of Branching and to Tumor Cells},
  number={9},
  volume={20},
  issn={1043-1802},
  journal={Bioconjugate chemistry},
  pages={1716--1728},
  author={André, Sabine and Specker, Daniel and Bovin, Nicolai V. and Lensch, Martin and Kaltner, Herbert and Gabius, Hans-Joachim and Wittmann, Valentin}
}

<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/123456789/9877">
    <dc:creator>Wittmann, Valentin</dc:creator>
    <dc:contributor>André, Sabine</dc:contributor>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T18:15:02Z</dcterms:available>
    <dc:contributor>Lensch, Martin</dc:contributor>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/9877/1/witt_045.pdf"/>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dc:contributor>Gabius, Hans-Joachim</dc:contributor>
    <dc:creator>Bovin, Nicolai V.</dc:creator>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dc:format>application/pdf</dc:format>
    <dc:rights>terms-of-use</dc:rights>
    <dc:language>eng</dc:language>
    <dcterms:title>Carbamate-Linked Lactose : Design of Clusters and Evidence for Selectivity to Block Binding of Human Lectins to (Neo)Glycoproteins with Increasing Degree of Branching and to Tumor Cells</dcterms:title>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/>
    <dc:creator>Specker, Daniel</dc:creator>
    <dcterms:issued>2009</dcterms:issued>
    <dc:contributor>Bovin, Nicolai V.</dc:contributor>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/9877"/>
    <dcterms:bibliographicCitation>First publ. in: Bioconjugate chemistry, 20 (2009), 9, pp. 1716 1728</dcterms:bibliographicCitation>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/>
    <dc:creator>Gabius, Hans-Joachim</dc:creator>
    <dc:contributor>Kaltner, Herbert</dc:contributor>
    <dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/>
    <dc:contributor>Specker, Daniel</dc:contributor>
    <dc:creator>Kaltner, Herbert</dc:creator>
    <dc:creator>Lensch, Martin</dc:creator>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/9877/1/witt_045.pdf"/>
    <dc:contributor>Wittmann, Valentin</dc:contributor>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T18:15:02Z</dc:date>
    <dcterms:abstract xml:lang="eng">Various pathogenic processes are driven by protein(lectin)-glycan interactions, especially involving β-galactosides at branch ends of cellular glycans. These emerging insights fuel the interest to design potent inhibitors to block lectins. As a step toward this aim, we prepared a series of ten mono- to tetravalent glycocompounds with lactose as a common headgroup. To obtain activated carbonate for ensuing carbamate formation, conditions for the facile synthesis of pure isomers from  nomerically unprotected lactose were identified. To probe for the often encountered intrafamily diversity of human lectins, we selected representative members from the three subgroups of adhesion/growth-regulatory galectins as receptors. Diversity of the glycan display was accounted for by using four (neo)glycoproteins with different degrees of glycan branching as matrices in solid-phase assays. Cases of increased inhibitory potency of lactose clusters compared to free lactose were revealed. Extent of relative inhibition was not directly associated with valency in the glycocompound and depended on the lectin type. Of note for screening protocols, efficacy of blocking appeared to decrease with increased degree of glycan branching in matrix glycoproteins. Binding to tumor cells was impaired with selectivity for galectins-3 and -4. Representative compounds did not impair growth of carcinoma cells up to a concentration of 5 mM of lactose moieties (valence-corrected value) per assay. The reported bioactivity and the delineation of its modulation by structural parameters of lectins and glycans set instructive examples for the further design of selective inhibitors and assay procedures.</dcterms:abstract>
    <dc:creator>André, Sabine</dc:creator>
  </rdf:Description>
</rdf:RDF>