Rational design of novel glycomimetics: Inhibitors of concanavalin A

Welch, Karen T.; Turner, Trent A.; Preast, Callie E.

doi:10.1016/j.bmcl.2008.09.095

Cited by 14 publications

(21 citation statements)

References 34 publications

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“…The main driving force between PG and PDDA, and between PDDA and Con A should be electrostatic interaction. As the best known lectin protein, Con A possesses a strong biospecific affinity with sugar groups [ 14 , 15 , 16 ]. The glycoenzyme GOD contains many glucose residues on the surface that can bind to Con A.…”

Section: Resultsmentioning

confidence: 99%

“…Con A is the best known member of the lectins and has been widely used as a representative lectin. Con A exists as a tetramer and each subunit contains a binding site to recognize the −OH group at the C-4 and C-6 sites of sugar molecules such as glucose and mannose, forming a highly specific 1:4 Con A-sugar complex [ 14 , 15 , 16 ]. For instance, in our previous work [ 17 ], Con A and horseradish peroxidase (HRP) with mannose residues on the surface were assembled into {Con A/HRP} n LbL films on electrodes by the biospecific interaction between them.…”

Section: Introductionmentioning

confidence: 99%

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A Stimuli-Responsive Biosensor of Glucose on Layer-by-Layer Films Assembled through Specific Lectin-Glycoenzyme Recognition

Yao

Gan

Peng

et al. 2016

Sensors

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The research on intelligent bioelectrocatalysis based on stimuli-responsive materials or interfaces is of great significance for biosensors and other bioelectronic devices. In the present work, lectin protein concanavalin A (Con A) and glycoenzyme glucose oxidase (GOD) were assembled into {Con A/GOD}n layer-by-layer (LbL) films by taking advantage of the biospecific lectin-glycoenzyme affinity between them. These film electrodes possess stimuli-responsive properties toward electroactive probes such as ferrocenedicarboxylic acid (Fc(COOH)2) by modulating the surrounding pH. The CV peak currents of Fc(COOH)2 were quite large at pH 4.0 but significantly suppressed at pH 8.0, demonstrating reversible stimuli-responsive on-off behavior. The mechanism of stimuli-responsive property of the films was explored by comparative experiments and attributed to the different electrostatic interaction between the films and the probes at different pH. This stimuli-responsive films could be used to realize active/inactive electrocatalytic oxidation of glucose by GOD in the films and mediated by Fc(COOH)2 in solution, which may establish a foundation for fabricating novel stimuli-responsive electrochemical biosensors based on bioelectrocatalysis with immobilized enzymes.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

A Stimuli-Responsive Biosensor of Glucose on Layer-by-Layer Films Assembled through Specific Lectin-Glycoenzyme Recognition

Yao

Gan

Peng

et al. 2016

Sensors

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“…The specific binding of Con A to glucan was verified by inhibiting the active binding site of Con A by adding α -methylglucoside (MG) to make sure that the assay signals resulted from glucan recognition and not from unspecific binding in mutans cultures [15]. Reference carbohydrates and supernatants of S. mutans cultures were coated in microtiter plates as described.…”

Section: Methodsmentioning

confidence: 99%

Dynamic Production of Soluble Extracellular Polysaccharides byStreptococcus mutans

Decker

Dietrich

Klein

et al. 2011

International Journal of Dentistry

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Caries development in the presence of Streptococcus mutans is associated not only with the production of extracellular water-insoluble polymers but also is based on water-soluble polysaccharides. The aim of this study was the evaluation of a novel glucan-specific Lectin assay for monitoring water-soluble EPS produced by S. mutans during several growth periods in different media. S. mutans cultures were grown for 24 h, 48 h, and 144 h in medium deficient of sucrose (A) and medium supplemented with 5% sucrose (B). Microtiter well plates were coated with cell-free supernatants followed by the addition of labeled Concanavalin-A and enzyme substrate. The substrate reactions were kinetically detected at 405 nm. The validation of the assay was performed using carbohydrates dextran, xanthan, and sucrose as reference. This new Concanavalin-A-based assay showed the highest sensitivity for dextran and revealed that the glucan production of S. mutans reached its maximum at 144 h in medium B according to bacterial maturation.

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“…Although the lectin‐related high‐throughput screening is mainly experimental, attention started to be devoted also towards lectin‐related virtual screening (e.g. concanavalin A132, 133 or selectins134). Large libraries of small molecules (either proprietary in‐house134 or free‐access from the National Cancer Institute (NCI) http://cactus.nci.nih.gov/ncidb2/download.html database) were used in these studies.…”

Section: Complementary “In Silico” Technologiesmentioning

confidence: 99%

Glycan and lectin microarrays for glycomics and medicinal applications

Katrlı́k

Švitel

Gemeiner

et al. 2010

Medicinal Research Reviews

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Three different array formats to study a challenging field of glycomics are presented here, based on the use of a panel of immobilized glycan or lectins, and on in silico computational approach. Glycan and lectin arrays are routinely used in combination with other analytical tools to decipher a complex nature of glycan-mediated recognition responsible for signal transduction of a broad range of biological processes. Fundamental aspects of the glycan and lectin array technology are discussed, with the focus on the choice and availability of the biorecognition elements, fabrication protocols, and detection platforms involved. Moreover, practical applications of both technologies especially in the field of clinical diagnostics are provided. The future potential of a complementary in silico array technology to reveal details of the protein-glycan-binding profiles is discussed here.

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Rational design of novel glycomimetics: Inhibitors of concanavalin A

Cited by 14 publications

References 34 publications

A Stimuli-Responsive Biosensor of Glucose on Layer-by-Layer Films Assembled through Specific Lectin-Glycoenzyme Recognition

A Stimuli-Responsive Biosensor of Glucose on Layer-by-Layer Films Assembled through Specific Lectin-Glycoenzyme Recognition

Dynamic Production of Soluble Extracellular Polysaccharides byStreptococcus mutans

Glycan and lectin microarrays for glycomics and medicinal applications

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