Source:http://linkedlifedata.com/resource/pubmed/id/17047869
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
21
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pubmed:dateCreated |
2006-10-18
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pubmed:abstractText |
The glycocalyx of eukaryotic cells is composed of glycoconjugates, which carry highly complex oligosaccharide portions. To elucidate the biological role and function of the glycocalyx in cell-cell communication and cellular adhesion processes, glycomimetics have become targets of glycosciences, which resemble the composition and structural complexity of the glycocalyx constituents. Here, we report about the synthesis of a class of oligosaccharide mimetics of a high-mannose type, which were obtained by mannosylation of spacered mono- and oligosaccharide cores. These carbohydrate-centered cluster mannosides have been targeted as inhibitors of mannose-specific bacterial adhesion, which is mediated by so-called type 1 fimbriae. Their inhibitory potencies were measured by ELISA and compared to methyl mannoside as well as to a series of mannobiosides, and finally to the polysaccharide mannan. The obtained results suggest a new interpretation of the mechanisms of bacterial adhesion according to a macromolecular rather than a multivalency effect.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1477-0520
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
7
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3901-12
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pubmed:meshHeading |
pubmed-meshheading:17047869-Bacterial Adhesion,
pubmed-meshheading:17047869-Biomimetic Materials,
pubmed-meshheading:17047869-Escherichia coli,
pubmed-meshheading:17047869-Fimbriae, Bacterial,
pubmed-meshheading:17047869-Glycosides,
pubmed-meshheading:17047869-Glycosylation,
pubmed-meshheading:17047869-Oligosaccharides
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pubmed:year |
2006
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pubmed:articleTitle |
Oligomannoside mimetics by glycosylation of 'octopus glycosides' and their investigation as inhibitors of type 1 fimbriae-mediated adhesion of Escherichia coli.
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pubmed:affiliation |
Otto Diels Institute of Organic Chemistry, Christiana Albertina University of Kiel, Otto-Hahn-Platz 4, 24098, Kiel, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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