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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
2001-3-23
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pubmed:abstractText |
An efficient and practical synthesis of cell adhesive glycopeptides exhibiting unique properties as a novel type of modulator of cellular recognition is described. A nonnatural glycopeptide 1 composed of sialyl Lewis x and Lys-Gly-Arg-Gly-Asp-Ser that interacts with both selectins and integrins has been systematically synthesized by combined chemical and enzymatic strategy. It is suggested that glycopeptide 1 showed much higher affinity with P-selectin (K(a) = 6.6 x 10(7) M(-1)) and E-selectin (K(a) = 4.5 x 10(5) M(-1)) than sialyl Lewis x. This compound also inhibited a specific interaction between human integrin beta(1) and its monoclonal antibody more effectively than the tetrapeptide Arg-Gly-Asp-Ser. Interestingly, it was demonstrated by surface plasmon resonance analysis that this heterobifunctional glycopeptide exhibited a capacity to form stable complexes with P-selectin and integrin beta(1) concurrently. It is also suggested that this activity can be used for the inhibition of integrin-mediated adhesion of activated helper T cells onto collagen-coated plates as a cell migration model. These results indicate that the chemoenzymatic hybridization strategy of different biological functions of carbohydrates and peptides is a new concept for designing potent glycoconjugates as antiinflammatory and anticancer metastasis reagents.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD29,
http://linkedlifedata.com/resource/pubmed/chemical/E-Selectin,
http://linkedlifedata.com/resource/pubmed/chemical/Fucosyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Glycopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Indicators and Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Integrins,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Oligosaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Selectins,
http://linkedlifedata.com/resource/pubmed/chemical/Sialyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/beta-galactoside...,
http://linkedlifedata.com/resource/pubmed/chemical/galactoside 3-fucosyltransferase
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0022-2623
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
44
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
715-24
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11262082-Animals,
pubmed-meshheading:11262082-Antibodies, Monoclonal,
pubmed-meshheading:11262082-Antigens, CD29,
pubmed-meshheading:11262082-Carbohydrate Sequence,
pubmed-meshheading:11262082-Cell Adhesion,
pubmed-meshheading:11262082-Cells, Cultured,
pubmed-meshheading:11262082-E-Selectin,
pubmed-meshheading:11262082-Fucosyltransferases,
pubmed-meshheading:11262082-Glycopeptides,
pubmed-meshheading:11262082-Humans,
pubmed-meshheading:11262082-Indicators and Reagents,
pubmed-meshheading:11262082-Integrins,
pubmed-meshheading:11262082-Kinetics,
pubmed-meshheading:11262082-Ligands,
pubmed-meshheading:11262082-Mice,
pubmed-meshheading:11262082-Models, Molecular,
pubmed-meshheading:11262082-Molecular Conformation,
pubmed-meshheading:11262082-Molecular Sequence Data,
pubmed-meshheading:11262082-Oligopeptides,
pubmed-meshheading:11262082-Oligosaccharides,
pubmed-meshheading:11262082-Selectins,
pubmed-meshheading:11262082-Sialyltransferases,
pubmed-meshheading:11262082-Surface Plasmon Resonance,
pubmed-meshheading:11262082-Th2 Cells
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pubmed:year |
2001
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pubmed:articleTitle |
Heterobifunctional ligands: practical chemoenzymatic synthesis of a cell adhesive glycopeptide that interacts with both selectins and integrins.
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pubmed:affiliation |
Division of Immunoregulation, Research Section of Disease Control, Institute for Genetic Medicine, Hokkaido University, Sapporo 060-0815, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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