Synthesis and Quantitative Evaluation of <i>Glycero</i>‐<scp>D</scp>‐<i>manno</i>‐heptose Binding to Concanavalin A by Fluorous‐Tag Assistance

Jaipuri, Firoz A.; Collet, Béatrice; Pohl, Nicola L. B.

doi:10.1002/ange.200704262

Cited by 18 publications

(8 citation statements)

References 35 publications

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“…Moreover, studies suggested that modifications at C-3, C-4, and C-6 positions of the d-mannopyranose deterred the binding to ConA [35]. In particular, the loss in the hydroxyl groups in the C-6 position as in 6-deoxy-d-mannose and 1,6-anhydro-␤-d-manno-pyranose result in complete loss of activity [35], unless the substitution of one of the hydrogen atoms in the C-6 position is a hydroxymethyl group [36], where the presence of a water molecule located near the C-6 hydroxy group of the nonreducing mannose helps mediate the interaction of the sugar with the lectin, stabilizing the nonreducing sugar to the protein (Asp 16) [35,37,38].…”

Section: Adsorption Behaviour Of Cona Onto Gml Thin Filmsmentioning

confidence: 97%

Galactomannan thin films as supports for the immobilization of Concanavalin A and/or dengue viruses

Valenga

Petri

Lucyszyn

et al. 2012

International Journal of Biological Macromolecules

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The immobilization of the glucose/mannose-binding lectin from Concanavalia ensiformis seeds (ConA) onto a monolayer made of a galactomannan extracted from Leucaena leucocephala seeds (GML), which was adsorbed onto - amino-terminated surfaces, was investigated by means of ellipsometry and atomic force microscopy. The mean thickness of GML monolayer, which polysaccharide consists of linear 1→4-linked β-D-mannopyranosil units partially substituted at C-6 by α-D-galactopyranosyl units, amounted to (1.5±0.2) nm. ConA molecules adsorbed onto GML surfaces forming (2.0±0.5) nm thick layers. However, in the presence of mannose the adsorption failed, indicating that ConA binding sites were blocked by mannose and were no longer available for mannose units present in the GML backbone. The GML film was also used as support for the adsorption of three serotypes of dengue virus particles (DENV-1, DENV-2 and DENV-3), where DENV-2 formed the thickest film (4±2) nm. The adsorbed layer of DENV-2 onto ConA-covered GML surfaces presented mean thickness values similar to that determined for DENV-2 onto bare GML surfaces. The addition of free mannose units prevented DENV-2 adsorption onto ConA-covered GML films by ~50%, suggesting competition between virus and mannose for ConA binding sites. This finding suggests that if ConA is also adsorbed to GML surface and its binding site is blocked by free mannose, virus particles are able to recognized GML mannose unities substituted by galactose. Interactions between polysaccharides thin films, proteins, and viruses are of great relevance since they can provide basis for the development of biotechnological devices. These results indicate that GML is a potential polysaccharide for biomaterials development, as those could involve interactions between ConA in immune system and viruses.

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Section: Adsorption Behaviour Of Cona Onto Gml Thin Filmsmentioning

confidence: 97%

Galactomannan thin films as supports for the immobilization of Concanavalin A and/or dengue viruses

Valenga

Petri

Lucyszyn

et al. 2012

International Journal of Biological Macromolecules

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“…21 In 1990, Chapleur and co-workers reported the synthesis of L-glycero-D-manno-heptose using the Ireland oxidative process as a vital component (Scheme 7). 21 In 1990, Chapleur and co-workers reported the synthesis of L-glycero-D-manno-heptose using the Ireland oxidative process as a vital component (Scheme 7).…”

Section: Synthesis Of L-glycero-d-manno-heptosementioning

confidence: 99%

The ‘Ireland’ one-pot alcohol oxidation coupling reactions: celebrating 30 years of diverse synthesis

Jeena

Robinson

2015

Org. Biomol. Chem.

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In 1985, Robert Ireland and co-worker were devising synthetic routes to polyether ionophore antibiotics and during this process several highly reactive aldehydes were encountered, which made their isolation and subsequent elaboration difficult. To circumvent this problem, the synthetic route commenced from the alcohol which was oxidized to the aldehyde and, to the crude mixture, was added the nucleophile. This procedure, dubbed the 'Ireland' oxidative process was found to be highly successful and adapted by many research groups the world over. As we celebrate 30 years since this landmark discovery, the following review will take a journey of the most innovative and wonderful applications of this process.

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“…[17] Glycoarrays (or carbohydrate microarrays) were reported in the early 2000s as a powerful tool for studying carbohydrateprotein interactions with minute amounts of material. [18][19][20][21][22][23][24][25][26][27][28][29][30][31][32][33][34][35][36][37] Microarrays have been reported for studying the enzymatic glycosylation of peptides [38][39][40] and glycosyltransferases. [41][42][43][44][45] However, to our knowledge, no carbohydrate microarrays have been implemented to study the activities and substrate specificities of glycosyl hydrolases and, more specifically, influenza neuraminidases.…”

Section: Introductionmentioning

confidence: 99%

Measurement of Enzymatic Activity and Specificity of Human and Avian Influenza Neuraminidases from Whole Virus by Glycoarray and MALDI‐TOF Mass Spectrometry

et al. 2011

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Influenza neuraminidases hydrolyze the ketosidic linkage between N-acetylneuraminic acid and its adjacent galactose residue in sialosides. This enzyme is a tetrameric protein that plays a critical role in the release of progeny virions. Several methods have been described for the determination of neuraminidase activity, usually based on colorimetric, fluorescent, or chemiluminescent detection. However, only a few of these tests allow discrimination of the sialyl-linkage specificity (i.e., α2-3- versus α2-6-linked sialyllactosides) of the neuraminidase. Herein we report a glycoarray-based assay and a MALDI-TOF study for assessing the activity and specificity of two influenza neuraminidases on whole viruses. The human A(H3N2) and avian A(H5N2) neuraminidase activities were investigated. The results from both approaches demonstrated that α2-3 sialyllactoside was a better substrate than α2-6 sialyllactoside for both viruses and that H5N2 virus had a lower hydrolytic activity than H3N2.

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Synthesis and Quantitative Evaluation of Glycero‐D‐manno‐heptose Binding to Concanavalin A by Fluorous‐Tag Assistance

Cited by 18 publications

References 35 publications

Galactomannan thin films as supports for the immobilization of Concanavalin A and/or dengue viruses

Galactomannan thin films as supports for the immobilization of Concanavalin A and/or dengue viruses

The ‘Ireland’ one-pot alcohol oxidation coupling reactions: celebrating 30 years of diverse synthesis

Measurement of Enzymatic Activity and Specificity of Human and Avian Influenza Neuraminidases from Whole Virus by Glycoarray and MALDI‐TOF Mass Spectrometry

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