“…The interaction between MAA and the 39-sialyllactose film gave a K d value of the same magnitude (K d MAA = 5.4 6 10 27 M). The obtained values are somewhat higher than literature values reported for different lectin systems ranging from 10 27 to 10 28 M. 60,82,83…”
Section: Specific and Non-specific Binding Of Lectins To The Oligosac...contrasting
This paper reports on the use of electrochemical surface plasmon resonance (E-SPR) for the detection of carbohydrate-binding proteins. The generation of an SPR sensor specific to lectins Arachis hypogaea (PNA) and Maackia amurensis (MAA) is based on the electrochemical polymerization of oligosaccharide derivatives functionalized by pyrrole groups. The resulting thin conducting polymer films were characterized using E-SPR and atomic force microscopy (AFM). The specific binding of PNA to polypyrrole-lactosyl and of MAA to polypyrrole-3'-sialyllactosyl films was investigated using SPR. The detection limit was 41 nM for PNA and 83 nM for MAA. Through Scatchard analysis and linear transformation of the SPR sensorgram data, association (k(ass)) and dissociation rate constants (k(diss)) could be determined.
“…The interaction between MAA and the 39-sialyllactose film gave a K d value of the same magnitude (K d MAA = 5.4 6 10 27 M). The obtained values are somewhat higher than literature values reported for different lectin systems ranging from 10 27 to 10 28 M. 60,82,83…”
Section: Specific and Non-specific Binding Of Lectins To The Oligosac...contrasting
This paper reports on the use of electrochemical surface plasmon resonance (E-SPR) for the detection of carbohydrate-binding proteins. The generation of an SPR sensor specific to lectins Arachis hypogaea (PNA) and Maackia amurensis (MAA) is based on the electrochemical polymerization of oligosaccharide derivatives functionalized by pyrrole groups. The resulting thin conducting polymer films were characterized using E-SPR and atomic force microscopy (AFM). The specific binding of PNA to polypyrrole-lactosyl and of MAA to polypyrrole-3'-sialyllactosyl films was investigated using SPR. The detection limit was 41 nM for PNA and 83 nM for MAA. Through Scatchard analysis and linear transformation of the SPR sensorgram data, association (k(ass)) and dissociation rate constants (k(diss)) could be determined.
“…10 Previously, we have compared the binding of several carbohydrate derivatives labeled with different reagents toward a lectin from Crocus sativus and found that the fluorescent groups introduced to the parent carbohydrates did not show obvious effect on the binding reaction. 12 In the present study, the total amounts of Con A and PAS-M 3 were 800 µg (7.7 nmol) and 5.0 µg (10 nmol), respectively.…”
Section: Binding Studies Between Concanavalin a And Pas-msupporting
confidence: 47%
“…10 Time-resolved fluorometry is also a powerful technique, 11 and has been applied to the analysis of the interaction of carbohydrate chains and a lectin from the bulbs of Crocus sativus. 12 Several papers concerning the determination of p-aminobenzoic acid and p-aminosalicylic acid in biological fluids have been reported. 13,14 These methods are based on the determination of the fluorescence arising from the formation of the complexes between aminobenzene derivatives and Tb 3+ .…”
We examined the formation of complexes between terbium ion (Tb3+) and carbohydrates labeled with aminobenzene compounds. Of the examined compounds, carbohydrates labeled with 4-aminosalicylic acid showed intense fluorescence with Tb3+ in the presence of cetylpyridinium chloride at pH 6.0. Calibration curves for maltose derivative showed good linearity between 5 pmol and at least 600 pmol, with good reproducibility. We applied the proposed technique to binding studies between manno-oligosaccharides and Concanavalin A.
“…The ESI-MS of 19 , showing typical ionic species at 2192.17 (M + H) + , 1118.60 (M + 2Na) 2+ , 1096.72 (M + 2H) 2+ , 1015.60 (M − Man + 2H) 2+ , 934.41 (M − 2Man + 2H) 2+ , 853.35 (M − 3Man + 2H) 2+ , 772.28 (M − 4Man + 2H) 2+ , 691.21 (M − 5Man + 2H) 2+ , 610.06 (M − 6Man + 2H) 2+ , is in good agreement with its structure. The procedure should be readily extendable to other native high-mannose type as well as complex type glyco-asparagine/glycopeptides, when their isolation from native glycoproteins is achievable ( , ). 1 Synthesis of Maleimide-Activated High Mannose Oligosaccharide…”
An array of maleimide-activated mono- and oligosaccharides were synthesized to permit site-specific glycosylation of cysteine-containing peptides and proteins. Maleimide-activated monosaccharides, in which the native alpha- or beta-O-glycosidic linkages found for nonreducing terminal sugars of native glycoproteins are preserved, were prepared using 2'-aminoethyl glycosides as the key intermediates. In addition, a native high-mannose type oligosaccharide, Man(9)GlcNAc(2)Asn, was converted into its maleimide-activated form by taking advantage of the existing amino group in the Asn portion. The application of these maleimide-activated carbohydrates was exemplified by the site-specific glycosylation of a 36-mer HIV-1 gp41 peptide, T20, which is a potent inhibitor against HIV infection. The chemoselective ligation was found to be rapid, highly efficient, and essentially quantitative. Tagging the biologically active peptide with a mannose and/or oligomannose moiety will be useful for targeting the drug to macrophage and dendritic cells, which are primary targets for HIV-1 infection and are expressing mannose- and oligomanose-specific receptors on their surface. In combination with site-specific mutagenesis, the maleimide-activated carbohydrates can serve as generally applicable tags for site-specific glycosylation of proteins via the highly efficient maleimide-thiol ligation reaction.
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