Lactose-containing starburst dendrimers: influence of dendrimer generation and binding-site orientation of receptors (plant/animal lectins and immunoglobulins) on binding properties.
Identifieur interne : 000032 ( Ncbi/Curation ); précédent : 000031; suivant : 000033Lactose-containing starburst dendrimers: influence of dendrimer generation and binding-site orientation of receptors (plant/animal lectins and immunoglobulins) on binding properties.
Auteurs : S. André [Allemagne] ; P J Ortega ; M A Perez ; R. Roy ; H J GabiusSource :
- Glycobiology [ 0959-6658 ] ; 1999.
Descripteurs français
- KwdFr :
- Animaux, Antigènes de différenciation (métabolisme), Bovins, Conformation des glucides, Données de séquences moléculaires, Galectine -3, Glycoconjugués (), Glycoconjugués (métabolisme), Glycoconjugués (pharmacologie), Humains, Hétérosides (métabolisme), Immunoglobuline G (métabolisme), Lactose (), Lectines (métabolisme), Liaison aux protéines, Ligands, Protéines inactivant les ribosomes de type 2, Protéines végétales, Préparations à base de plantes, Récepteurs de surface cellulaire (métabolisme), Sites de fixation, Souris, Séquence glucidique, Thermodynamique, Toxines biologiques (métabolisme).
- MESH :
- métabolisme : Antigènes de différenciation, Glycoconjugués, Hétérosides, Immunoglobuline G, Lectines, Récepteurs de surface cellulaire, Toxines biologiques.
- pharmacologie : Glycoconjugués.
- Animaux, Bovins, Conformation des glucides, Données de séquences moléculaires, Galectine -3, Glycoconjugués, Humains, Lactose, Liaison aux protéines, Ligands, Protéines inactivant les ribosomes de type 2, Protéines végétales, Préparations à base de plantes, Sites de fixation, Souris, Séquence glucidique, Thermodynamique.
English descriptors
- KwdEn :
- Animals, Antigens, Differentiation (metabolism), Binding Sites, Carbohydrate Conformation, Carbohydrate Sequence, Cattle, Galectin 3, Glycoconjugates (chemistry), Glycoconjugates (metabolism), Glycoconjugates (pharmacology), Glycosides (metabolism), Humans, Immunoglobulin G (metabolism), Lactose (chemistry), Lectins (metabolism), Ligands, Mice, Molecular Sequence Data, Plant Preparations, Plant Proteins, Protein Binding, Receptors, Cell Surface (metabolism), Ribosome Inactivating Proteins, Type 2, Thermodynamics, Toxins, Biological (metabolism).
- MESH :
- chemical , chemistry : Glycoconjugates, Lactose.
- chemical , metabolism : Antigens, Differentiation, Glycoconjugates, Glycosides, Immunoglobulin G, Lectins, Receptors, Cell Surface, Toxins, Biological.
- chemical , pharmacology : Glycoconjugates.
- Animals, Binding Sites, Carbohydrate Conformation, Carbohydrate Sequence, Cattle, Galectin 3, Humans, Ligands, Mice, Molecular Sequence Data, Plant Preparations, Plant Proteins, Protein Binding, Ribosome Inactivating Proteins, Type 2, Thermodynamics.
Abstract
Starburst glycodendrimers offer the potential to serve as high-affinity ligands for clinically relevant sugar receptors. In order to define areas of application, their binding behavior towards sugar receptors with differential binding-site orientation but identical monosaccharide specificity must be evaluated. Using poly(amidoamine) starburst dendrimers of five generations, which contain the p-isothiocyanato derivative of p-aminophenyl-beta-D-lactoside as ligand group, four different types of galactoside-binding proteins were chosen for this purpose, i.e., the (AB)(2)-toxic agglutinin from mistletoe, a human immunoglobulin G fraction, the homodimeric galectin-1 with its two binding sites at opposite ends of the jelly-roll-motif-harboring protein and monomeric galectin-3. Direct solid-phase assays with surface-immobilized glycodendrimers resulted in obvious affinity enhancements by progressive core branching for the plant agglutinin and less pronounced for the antibody and galectin-1. High density of binding of galectin-3 with modest affinity increases only from the level of the 32-mer onwards points to favorable protein-protein interactions of the monomeric lectin and a spherical display of the end groups without a major share of backfolding. When the inhibitory potency of these probes was evaluated as competitor of receptor binding to an immobilized neoglycoprotein or to asialofetuin, a marked selectivity was detected. The 32- and 64-mers were second to none as inhibitors for the plant agglutinin against both ligand-exposing matrices and for galectin-1 on the matrix with a heterogeneous array of interglycoside distances even on the per-sugar basis. In contrast, a neoglycoprotein with the same end group was superior in the case of the antibody and, less pronounced, monomeric galectin-3. Intimate details of topological binding-site presentation and the ligand display on different generations of core assembly are major operative factors which determine the potential of dendrimers for applications as lectin-targeting device, as attested by these observations.
DOI: 10.1093/glycob/9.11.1253
PubMed: 10536041
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pubmed:10536041Le document en format XML
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André</name><affiliation wicri:level="4"><nlm:affiliation>Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University, Veterinärstrasse 13, D-80539 Munich, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University, Veterinärstrasse 13, D-80539 Munich</wicri:regionArea><placeName><region type="land" nuts="1">Bavière</region><region type="district" nuts="2">District de Haute-Bavière</region><settlement type="city">Munich</settlement></placeName><orgName type="university">Université Louis-et-Maximilien de Munich</orgName></affiliation></author><author><name sortKey="Ortega, P J" sort="Ortega, P J" uniqKey="Ortega P" first="P J" last="Ortega">P J Ortega</name></author><author><name sortKey="Perez, M A" sort="Perez, M A" uniqKey="Perez M" first="M A" last="Perez">M A Perez</name></author><author><name sortKey="Roy, R" sort="Roy, R" uniqKey="Roy R" first="R" last="Roy">R. 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André</name><affiliation wicri:level="4"><nlm:affiliation>Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University, Veterinärstrasse 13, D-80539 Munich, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University, Veterinärstrasse 13, D-80539 Munich</wicri:regionArea><placeName><region type="land" nuts="1">Bavière</region><region type="district" nuts="2">District de Haute-Bavière</region><settlement type="city">Munich</settlement></placeName><orgName type="university">Université Louis-et-Maximilien de Munich</orgName></affiliation></author><author><name sortKey="Ortega, P J" sort="Ortega, P J" uniqKey="Ortega P" first="P J" last="Ortega">P J Ortega</name></author><author><name sortKey="Perez, M A" sort="Perez, M A" uniqKey="Perez M" first="M A" last="Perez">M A Perez</name></author><author><name sortKey="Roy, R" sort="Roy, R" uniqKey="Roy R" first="R" last="Roy">R. Roy</name></author><author><name sortKey="Gabius, H J" sort="Gabius, H J" uniqKey="Gabius H" first="H J" last="Gabius">H J Gabius</name></author></analytic><series><title level="j">Glycobiology</title><idno type="ISSN">0959-6658</idno><imprint><date when="1999" type="published">1999</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Antigens, Differentiation (metabolism)</term><term>Binding Sites</term><term>Carbohydrate Conformation</term><term>Carbohydrate Sequence</term><term>Cattle</term><term>Galectin 3</term><term>Glycoconjugates (chemistry)</term><term>Glycoconjugates (metabolism)</term><term>Glycoconjugates (pharmacology)</term><term>Glycosides (metabolism)</term><term>Humans</term><term>Immunoglobulin G (metabolism)</term><term>Lactose (chemistry)</term><term>Lectins (metabolism)</term><term>Ligands</term><term>Mice</term><term>Molecular Sequence Data</term><term>Plant Preparations</term><term>Plant Proteins</term><term>Protein Binding</term><term>Receptors, Cell Surface (metabolism)</term><term>Ribosome Inactivating Proteins, Type 2</term><term>Thermodynamics</term><term>Toxins, Biological (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Antigènes de différenciation (métabolisme)</term><term>Bovins</term><term>Conformation des glucides</term><term>Données de séquences moléculaires</term><term>Galectine -3</term><term>Glycoconjugués ()</term><term>Glycoconjugués (métabolisme)</term><term>Glycoconjugués (pharmacologie)</term><term>Humains</term><term>Hétérosides (métabolisme)</term><term>Immunoglobuline G (métabolisme)</term><term>Lactose ()</term><term>Lectines (métabolisme)</term><term>Liaison aux protéines</term><term>Ligands</term><term>Protéines inactivant les ribosomes de type 2</term><term>Protéines végétales</term><term>Préparations à base de plantes</term><term>Récepteurs de surface cellulaire (métabolisme)</term><term>Sites de fixation</term><term>Souris</term><term>Séquence glucidique</term><term>Thermodynamique</term><term>Toxines biologiques (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glycoconjugates</term><term>Lactose</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Antigens, Differentiation</term><term>Glycoconjugates</term><term>Glycosides</term><term>Immunoglobulin G</term><term>Lectins</term><term>Receptors, Cell Surface</term><term>Toxins, Biological</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Glycoconjugates</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Antigènes de différenciation</term><term>Glycoconjugués</term><term>Hétérosides</term><term>Immunoglobuline G</term><term>Lectines</term><term>Récepteurs de surface cellulaire</term><term>Toxines biologiques</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Glycoconjugués</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Binding Sites</term><term>Carbohydrate Conformation</term><term>Carbohydrate Sequence</term><term>Cattle</term><term>Galectin 3</term><term>Humans</term><term>Ligands</term><term>Mice</term><term>Molecular Sequence Data</term><term>Plant Preparations</term><term>Plant Proteins</term><term>Protein Binding</term><term>Ribosome Inactivating Proteins, Type 2</term><term>Thermodynamics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Bovins</term><term>Conformation des glucides</term><term>Données de séquences moléculaires</term><term>Galectine -3</term><term>Glycoconjugués</term><term>Humains</term><term>Lactose</term><term>Liaison aux protéines</term><term>Ligands</term><term>Protéines inactivant les ribosomes de type 2</term><term>Protéines végétales</term><term>Préparations à base de plantes</term><term>Sites de fixation</term><term>Souris</term><term>Séquence glucidique</term><term>Thermodynamique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Starburst glycodendrimers offer the potential to serve as high-affinity ligands for clinically relevant sugar receptors. In order to define areas of application, their binding behavior towards sugar receptors with differential binding-site orientation but identical monosaccharide specificity must be evaluated. Using poly(amidoamine) starburst dendrimers of five generations, which contain the p-isothiocyanato derivative of p-aminophenyl-beta-D-lactoside as ligand group, four different types of galactoside-binding proteins were chosen for this purpose, i.e., the (AB)(2)-toxic agglutinin from mistletoe, a human immunoglobulin G fraction, the homodimeric galectin-1 with its two binding sites at opposite ends of the jelly-roll-motif-harboring protein and monomeric galectin-3. Direct solid-phase assays with surface-immobilized glycodendrimers resulted in obvious affinity enhancements by progressive core branching for the plant agglutinin and less pronounced for the antibody and galectin-1. High density of binding of galectin-3 with modest affinity increases only from the level of the 32-mer onwards points to favorable protein-protein interactions of the monomeric lectin and a spherical display of the end groups without a major share of backfolding. When the inhibitory potency of these probes was evaluated as competitor of receptor binding to an immobilized neoglycoprotein or to asialofetuin, a marked selectivity was detected. The 32- and 64-mers were second to none as inhibitors for the plant agglutinin against both ligand-exposing matrices and for galectin-1 on the matrix with a heterogeneous array of interglycoside distances even on the per-sugar basis. In contrast, a neoglycoprotein with the same end group was superior in the case of the antibody and, less pronounced, monomeric galectin-3. Intimate details of topological binding-site presentation and the ligand display on different generations of core assembly are major operative factors which determine the potential of dendrimers for applications as lectin-targeting device, as attested by these observations.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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