A comparison of biological and calorimetric analyses of multivalent glycodendrimer ligands for concanavalin A

Corbell, Jayme B.; Lundquist, Joseph J.; Toone, Eric J.

doi:10.1016/s0957-4166(99)00589-3

Cited by 104 publications

(91 citation statements)

References 50 publications

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“…The diminution of −DH was therefore considered the thermodynamic signature for the intermolecular aggregation process. 91, 97 Studies previously carried out by Toone and co-workers employing another series of dendritic multivalent ligands, 96 where crystals of both bi-and trivalent ligands were grown in the presence of succinylated Con A, showed that the carbohydrate orientation within the binding site was identical to that of the corresponding monovalent ligand. Interestingly, ligands with valencies greater than three showed affinity enhancements in agglutination assay but not by ITC.…”

Section: Multivalent Ligandsmentioning

confidence: 96%

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Lectins: Tools for the Molecular Understanding of the Glycocode

2005

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Recent progress in glycobiology has revealed that cell surface oligosaccharides play an essential role in recognition events. More precisely, these saccharides may be complexed by lectins, carbohydrate-binding proteins other than enzymes and antibodies, able to recognise sugars in a highly specific manner. The ubiquity of lectin-carbohydrate interactions opens enormous potential for their exploitation in BA (1993) and DPhil (1996) T h i s j o u r n a l i s © T h e R o y a l S o c i e t y o f C h e m i s t r y

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Section: Multivalent Ligandsmentioning

confidence: 96%

“…4 with the same lectin. 97 The corresponding thermodynamic binding parameters are reported in regular type in Table 4.…”

Section: Multivalent Ligandsmentioning

confidence: 99%

Lectins: Tools for the Molecular Understanding of the Glycocode

2005

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“…[30][31][32][33][34] Microtiter plates are coated with a reference ligand (often a (neo)glycoprotein or polysaccharide) and IC 50 values for inhibition of the binding of an enzyme-labeled lectin to the immobilized reference ligand (the matrix) by the soluble ligands to be tested are determined. The advantage of ELLA compared to solid-phase binding assays such as surface plasmon resonance (SPR) 35 is that both, lectin and ligand are in solution.…”

Section: Introductionmentioning

confidence: 99%

Probing multivalent carbohydrate–lectin interactions by an enzyme-linked lectin assay employing covalently immobilized carbohydrates

Maierhofer

Rohmer

Wittmann

2007

Bioorganic & Medicinal Chemistry

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Abstract-We report here the synthesis of a series of mono-to trivalent N-acetylglucosamine (GlcNAc) derivatives as ligands for the plant lectin wheat germ agglutinin (WGA). Their WGA binding potencies were determined by an established enzyme-linked lectin assay (ELLA) employing microtiter plates with non-covalently immobilized porcine stomach mucin (PSM) as reference ligand and an ELLA with a new GlcNAc derivative covalently immobilized via a thiourea linkage. Comparison of both assays revealed that the type of presentation of GlcNAc residues on the microtiter plates either as part of a glycoprotein or as a covalently immobilized monosaccharide derivative strongly influences the outcome of the assay. Although the apparent dissociation constants K ELLA D for the interaction of peroxidase-labeled WGA with the microtiter plates are comparable for both surfaces, IC 50 values obtained with the PSM-free ELLA were substantially lower. Even more strikingly, this ELLA displayed a better differentiation between ligands of different valency leading to significantly higher relative inhibitory potencies of multivalent ligands compared to monovalent. Additionally, problems associated with the use of PSM, such as maximum inhibition at considerably less than 100% and poor reproducibility of IC 50 values could be overcome with this type of ELLA.

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“…There are various glyco-materials with glyco-clusters such as glycopolymer [7,8] and glycodendrimers [9,10], which can be utilized as biomaterials. Recently, much attention has been paid to sugar microarrays because glyco-materials can realize the high-throughput analyses of proteins and cells [11,12].…”

Section: Introductionmentioning

confidence: 99%

Sugar microarray via click chemistry: molecular recognition with lectins and amyloid β (1–42)

Matsumoto

Yamauchi

Fukuda

et al. 2009

Science and Technology of Advanced Materials

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Sugar microarrays were fabricated on various substrates via click chemistry. Acetylene-terminated substrates were prepared by forming self-assembled monolayers (SAMs) on a gold substrate with alkyl-disulfide and on silicon, quartz and glass substrates with a silane-coupling reagent. The gold substrates were subjected to surface plasmon resonance measurements, and the quartz and glass substrates were subjected to spectroscopy measurements and optical microscopy observation. The saccharide-immobilized substrate on the gold substrate showed specific interaction with the corresponding lectin, and the saccharides showed inert surface properties to other proteins with a high signal-to-noise ratio. We also focused on the saccharide-protein interaction on protein amyloidosis of Alzheimer amyloid β. Amyloid β peptide showed conformation transition on the saccharide-immobilization substrate into a β-sheet, and fibril formation and amyloid aggregates were found on the specific saccharides.

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A comparison of biological and calorimetric analyses of multivalent glycodendrimer ligands for concanavalin A

Cited by 104 publications

References 50 publications

Lectins: Tools for the Molecular Understanding of the Glycocode

Lectins: Tools for the Molecular Understanding of the Glycocode

Probing multivalent carbohydrate–lectin interactions by an enzyme-linked lectin assay employing covalently immobilized carbohydrates

Sugar microarray via click chemistry: molecular recognition with lectins and amyloid β (1–42)

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