Analysis of the interaction between lectins and tetra- and tri-saccharide mimics of the Sda determinant by surface plasmon resonance detection

Blanco, José L. Jiménez; Haseley, Simon R.; Kamerling, Johannis P.; Vliegenthart, Johannes F.G.

doi:10.1016/s0300-9084(01)01302-5

Cited by 10 publications

(5 citation statements)

References 29 publications

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“…Previous work examining antibody binding to similar epitopes used solid phase enzyme immunoassay or microcalorimetry. , These studies, while effective, required numerous steps and significant quantities of samples. SPR has been used in numerous carbohydrate binding studies, − and there have been several reports on the use of SPR imaging as a label-free detection platform for carbohydrate arrays. ,− Relevant to the present work, SPR imaging was used to screen serum antibody binding to an array of natural glycans. The glycans were covalently immobilized to an epoxide modified chip .…”

Section: Introductionmentioning

confidence: 94%

“…23,24 These studies, while effective, required numerous steps and significant quantities of samples. SPR has been used in numerous carbohydrate binding studies, [25][26][27][28][29][30][31][32] and there have been several reports on the use of SPR imaging as a label-free detection platform for carbohydrate arrays. 30,[33][34][35][36] Relevant to the present work, SPR imaging was used to screen serum antibody binding to an array of natural glycans.…”

Section: Introductionmentioning

confidence: 99%

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Optimization of Immobilized Bacterial Disaccharides for Surface Plasmon Resonance Imaging Measurements of Antibody Binding

Grant

Kanda

et al. 2008

Langmuir

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The interactions between proteins and immobilized carbohydrates are crucial to biological events such as cell signaling and immune response. The modification of surfaces with carbohydrates to create sensing platforms provides a pathway to study these interactions in a laboratory setting. In this work, a family of structurally related Salmonella disaccharide epitopes is immobilized on thin gold films in an array format to probe antibody binding with surface plasmon resonance (SPR) imaging. The disaccharides are modified with an alkyl thiol linker for facile immobilization to gold. Small differences in the stereochemistry of the immobilized, modified disaccharides are shown to greatly influence the binding of a monoclonal antibody. Specifically, binding is only observed to an immobilized abequose dideoxyhexose relative to a tyvelose or a paratose analogue. However, both the amount and relative strength of bound antibody depends on the distribution of disaccharide moieties in a mixed monolayer of the epitope and a nonbinding diluent molecule. We thoroughly characterize the mixed monolayers with a variety of techniques to understand the optimal density and distribution of the disaccharide for antibody capture. This work reinforces the importance of controlling the density of ligands at the interface for optimized surface based bioassays.

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Section: Introductionmentioning

confidence: 94%

Section: Introductionmentioning

confidence: 99%

Optimization of Immobilized Bacterial Disaccharides for Surface Plasmon Resonance Imaging Measurements of Antibody Binding

Grant

Kanda

et al. 2008

Langmuir

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“…SPR-based sensors detect in real time refractive index (RI) changes of the medium adjacent to the sensor surface and sense to a depth of ∼200 nm from the sensor surface. Therefore, it has been used, for instance, to follow interactions between polysaccharides and biomolecules − or between polymers and biomolecules, , to monitor surface protection against protein adsorption, , and to detect the in-situ conformational changes of macromolecules and biomolecules …”

Section: Introductionmentioning

confidence: 99%

Surface Plasmon Resonance Study of the Interaction of a β-Cyclodextrin Polymer and Hydrophobically Modified Poly(N-isopropylacrylamide)

Wintgens

2005

Langmuir

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Surface plasmon resonance (SPR) technique is used to follow, both in real time and in situ, the association between a physically adsorbed polymer of beta-cyclodextrin (pbetaCD) and different hydrophobically modified poly(N-isopropylacrylamide) (PNIPAM) copolymers containing either adamantyl or dodecyl groups. This association is due to the complex formation between the hydrophobic groups and the betaCD cavities. Therefore, the adsorbed amount of PNIPAM onto the pbetaCD layer depends on the substituent and on its substitution level. The association and dissociation rate constants are evaluated from the kinetics of PNIPAM adsorption. An estimation of the association constants leads to values higher than 10(4) M(-1), reflecting the strong interaction between these polymers.

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“…GlGp1 also showed a binding activity to WGA. WGA has been used in several SPR studies for carbohydrate-protein interaction analysis [44,45]. Different buffer systems, at pH 5.0 and 7.4, respectively, were used to compare the binding behaviour between ConA and WGA and to apply the optimized conditions routinely used for preparative WGA affinity separations [46].…”

Section: Discussionmentioning

confidence: 99%

Isolation of a cytotoxic glycoprotein from the Scyphozoa Cyanea lamarckii by lectin-affinity chromatography and characterization of molecule interactions by surface plasmon resonance

Helmholz¹,

Naatz

Lassen³

et al. 2008

Journal of Chromatography B

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A biospecific lectin-affinity-based isolation process for a novel glycoprotein (ClGp1) from the venom of the pelagic jellyfish Cyanea lamarckii, is described and the isolated glycoprotein is chemically and biologically characterized according to size, molecular interaction and toxicity. The molecular mass of the isolated protein is 25.7 kDa as determined by matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF). The carbohydrate content was calculated after enzymatic deglycosylation as 6.85 kDa. The glycoprotein is cytotoxic and could be isolated from cnidocysts of mesenteric and fishing tentacles. The binding behaviour of the glycoprotein to the lectins Concanavalin A (ConA) and Wheat Germ Agglutinin (WGA) was analyzed by surface plasmon resonance (SPR) and affinity constants in the range of K(D)=3.0 x 10(-7) M for ConA and 2.1 x 10(-6) M (pH 5.0) and 2.6 x 10(-6) M (pH 7.4) for WGA were obtained.

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Analysis of the interaction between lectins and tetra- and tri-saccharide mimics of the Sda determinant by surface plasmon resonance detection

Abstract: -The binding properties of a spacer

Cited by 10 publications

References 29 publications

Optimization of Immobilized Bacterial Disaccharides for Surface Plasmon Resonance Imaging Measurements of Antibody Binding

Optimization of Immobilized Bacterial Disaccharides for Surface Plasmon Resonance Imaging Measurements of Antibody Binding

Surface Plasmon Resonance Study of the Interaction of a β-Cyclodextrin Polymer and Hydrophobically Modified Poly(N-isopropylacrylamide)

Isolation of a cytotoxic glycoprotein from the Scyphozoa Cyanea lamarckii by lectin-affinity chromatography and characterization of molecule interactions by surface plasmon resonance

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