Design of carbohydrate multiarrays

Dyukova, V.I.; Шилова, Н. В.; Galanina, Oxana; Rubina, A. Yu.; Bovin, Nicolai V.

doi:10.1016/j.bbagen.2005.12.005

Cited by 59 publications

(43 citation statements)

References 28 publications

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“…In contrast to template-encoded nucleic acid and protein sequences which aid function assignments, the need for a more empirical, high throughput analysis of potential carbohydrate binding partners has resulted in a variety of approaches for the generation of carbohydrate microarrays [2][3][4][5][6]. For reasons of sensitivity, throughput and compatibility with existing nucleic acid array hardware, fluorescence based measurements is, to date, the prevalent detection principle for such microarrays.…”

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confidence: 98%

Surface plasmon resonance imaging for real-time, label-free analysis of protein interactions with carbohydrate microarrays

et al. 2007

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Plant lectin recognition of glycans was evaluated by SPR imaging using a model array of N-biotinylated aminoethyl glycosides of beta-D-glucose (negative control), alpha-D: -mannose (conA-responsive), beta-D-galactose (RCA(120)-responsive) and N-acetyl-beta-D-: glucosamine (WGA-responsive) printed onto neutravidin-coated gold chips. Selective recognition of the cognate ligand was observed when RCA(120) was passed over the array surface. Limited or no binding was observed for the non-cognate ligands. SPR imaging of an array of 40 sialylated and unsialylated glycans established the binding preference of hSiglec7 for alpha2-8-linked disialic acid structures over alpha2-6-sialyl-LacNAcs, which in turn were recognized and bound with greater affinity than alpha2-3-sialyl-LacNAcs. Affinity binding data could be obtained with as little as 10-20 microg of lectin per experiment. The SPR imaging technique was also able to establish selective binding to the preferred glycan ligand when analyzing crude culture supernatant containing 10-20 microg of recombinant hSiglec7-Fc. Our results show that SPR imaging provides results that are in agreement with those obtained from fluorescence based carbohydrate arrays but with the added advantage of label-free analysis.

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confidence: 98%

Surface plasmon resonance imaging for real-time, label-free analysis of protein interactions with carbohydrate microarrays

et al. 2007

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“…For example, it was reported that an ordinary microarray scanner can collect signals in a scope from the substrate surface to a height of more than 20 µm, so the particles with the size between tens and several hundred of nanometers should be suitable for the microarray analysis. 8,32 The fluorescence image (Figure 7) scanned by a confocal microarray scanner was an early test to use the carbohydrate affinity particles in this field. Though this analysis gave some meaningful results, presently, it still lacked reliability and accuracy comparing with the former protein binding experiment.…”

Section: 62mentioning

confidence: 99%

“…Generally speaking, the strategies for coating the carbohydrates onto a certain solid support can be classified into three categories: 8,9 physical adsorption, streptavidin/biotin immobilization, and chemical attachment. Nitrocellulose and black polystyrene films were commonly used for non-covalent adsorption of the polysaccharides and glycoproteins.…”

Section: Introductionmentioning

confidence: 99%

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Carbohydrate Coated Polymer Particles: Preparation and Protein‐binding Studies

et al. 2011

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A facile and effective organic synthesis route was provided for preparation of the carbohydrate coated polymer small particles. First, amino-activated particles were prepared from PAN (polyacrylonitrile) by the heterogeneous cross-linking method, then the amino groups on the particle were converted into hydrazide groups by N-alkylation and hydrazine activation, meanwhile the length of linker was prolonged to the designed value. FTIR (Fourier Transform Infrared Spectroscopy) was used to study the reactions in the synthesis steps and to optimize part of the synthesis conditions. Two carbohydrates (maltose and heparin) were then directly coupled to the hydrazide-activated particles in a relative high yield, the obtained particles were used to interact with BSA (bovine serum albumin) and typical heparin-binding proteins. All of these particles had some nonspecific interactions with proteins and heparin coated particles showed additional strong binding ability with the heparin-binding proteins. Data also showed that a longer linker length not only weakened nonspecific interaction but also increased the specific binding ability. As the carbohydrate coated particles are independent, flexible and easily detectable, they should be good acceptors for the diverse bioactive studies of carbohydrates.

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“…Although analytes can be detected by a wide range of immobilized ligands, such as antibodies (Soh et al, 2003;Liu et al, 2004;Choi et al, 2005;Muller-Renaud et al, 2005), enzymes, and carbohydrate-binding proteins (CBPs) (Hsieh et al, 2004), the development of carbohydrate-based biosensors has recently received increased attention because of the importance of carbohydrate-protein interactions in life. So far, carbohydratebased biosensors are predominantly used for the characterization of the kinetics and affinity of carbohydrate-protein interactions (Shinohara et al, 1994;Bourne et al, 2002;Zhang et al, 2006), or in an array-type set-up (Love and Seeberger, 2002;Feizi et al, 2003;Blixt et al, 2004;Dyukova et al, 2006) to determine the specificity, and possible cross-reactivity of a CBP. However, it would also be of interest to apply carbohydrate-based biosensors to the sensitive detection and quantification of minute amounts of CBPs, which could lead to the development of diagnostic tools.…”

Section: Introductionmentioning

confidence: 99%

The application of neoglycopeptides in the development of sensitive surface plasmon resonance-based biosensors

Maljaars

Souza

Halkes

et al. 2008

Biosensors and Bioelectronics

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a b s t r a c tThe development of a biosensor based on surface plasmon resonance is described for the detection of carbohydrate-binding proteins in solution on a Biacore 2000 instrument, using immobilized glycopeptides as ligands. Their selection was based on previous screenings of solid-phase glycopeptide libraries with Ricinus communis agglutinin (RCA 120 ) and human adhesion/growth-regulatory galectin-1 (h-Gal-1). Glycopeptides were immobilized on Au sensor chips functionalized with mixed self-assembled monolayers of different ratios of 11-mercapto-1-undecanol and 11-mercaptoundecanoic acid, and of 3-mercapto-1-propanol and 11-mercaptoundecanoic acid. The biosensors were optimized for the detection of RCA 120 , and a detection limit of 0.13 nM was obtained. Subsequent experiments with h-Gal-1 indicated a detection limit of at least 0.9 nM for this lectin. Additionally, the effect of interfering proteins on the sensitivity of the optimized biosensor was investigated.

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Design of carbohydrate multiarrays

Cited by 59 publications

References 28 publications

Surface plasmon resonance imaging for real-time, label-free analysis of protein interactions with carbohydrate microarrays

Surface plasmon resonance imaging for real-time, label-free analysis of protein interactions with carbohydrate microarrays

Carbohydrate Coated Polymer Particles: Preparation and Protein‐binding Studies

The application of neoglycopeptides in the development of sensitive surface plasmon resonance-based biosensors

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