Interaction assay of oligosaccharide with lectins using glycosylasparagine

Mizuno, Mamoru; Noguchi, Midori; Imai, Mie; Motoyoshi, Tetsuya; Inazu, Toshiyuki

doi:10.1016/j.bmcl.2003.10.035

Cited by 26 publications

(17 citation statements)

References 28 publications

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“…The obtained K a value is comparable with that presented elsewhere (K a = 0.1−3 × 10 6 M −1 [33]; K a = 1.7 × 10 6 M −1 [14]; K a = 0.3 × 10 6 M −1 [34]). The force spectroscopy mode of AFM enables one also to explore the energy landscape of dissociation pathway from the low-energy (bound complex) to the high-energy states (unbound) through the transition state.…”

Section: Methods Dissociation Rate Constantsupporting

confidence: 77%

“…CaY is a glycoprotein containing the mannose type of ligand specifically recognized by the lectin concanavalin A. The high affinity of Con A to specific sugar residues is useful not only for characterization of malignant cells [12], but also in different types of bioassays for studying the glycoprotein and carbohydrate recognition processes [13,14]. Our previous AFM study has shown the successful identification of the specific Con ACaY interaction by means of force spectroscopy [10].…”

Section: Introductionmentioning

confidence: 99%

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Atomic Force Microscopy and Quartz Crystal Microbalance Study of the Lectin-Carbohydrate Interaction Kinetics

et al. 2007

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Two analytical methods, atomic force microscopy and quartz crystal microbalance, were applied to the study of the reaction kinetics occurring between concanavalin A and carboxypeptidase Y, presenting the specific lectin-carbohydrate recognition. The dissociation rate constants for concanavalin A-carboxypeptidase Y complex obtained using both atomic force microscopy and quartz crystal microbalance were of the same order of magnitude: k diss = 0.170 ± 0.060 s −1 and k diss = 0.095 ± 0.002 s −1 , respectively. In addition, each method alone aided in determining other parameters characterizing the studied interaction. Quartz crystal microbalance permitted us to estimate the association rate (k ass = (5.6 ± 0.1) × 10 4 M −1 s −1 ) and the equilibrium (Ka = (0.59 ± 0.01) × 10 6 M −1 ) constants for the binding process occurring between concanavalin A and mannose residues of carboxypeptidase Y under given experimental conditions. Atomic force microscopy in force spectroscopy mode enabled the determination of the energy barrier position of r = 2.29 ± 0.04Å characterizing the dissociation of concanavalin Acarboxypeptidase Y molecular complex. The presented results show that both atomic force microscopy and quartz crystal microbalance can be used to determine quantitative parameters characterizing the specific molecular interaction. Both methods can be easily combined for complementary and/or alternative studies of a chosen molecular interaction. By preparing the samples in the same manner the direct comparison between the data obtained via atomic force microscopy and quartz crystal microbalance can be made.

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Section: Methods Dissociation Rate Constantsupporting

confidence: 77%

Section: Introductionmentioning

confidence: 99%

Atomic Force Microscopy and Quartz Crystal Microbalance Study of the Lectin-Carbohydrate Interaction Kinetics

et al. 2007

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“…(5)) used in our work gave an even smaller value of the association constant, (0.57 ± 0.02) × 10 6 M −1 , lying outside the range of reported values of association constants of Con A-mannose binding [24,37,40,41]. However, in the present measurements, lectin molecules were immobilized on a surface, while in the abovementioned works [24,27,40,41], they were free in a solution. This difference should strongly influence the association constant value.…”

Section: Discussioncontrasting

confidence: 68%

“…It was shown that the association constant for binding between the Con A and the oligosaccharides with a total number of mannose ligands greater than 6 should exceed the value of 1 × 10 6 M −1 [39]. The association equilibrium constant reported so far for specific interaction of Con A with oligosaccharides containing mannose residues ranged from 2 × 10 6 to 30 × 10 6 M −1 , depending on the type of ligands studied [24,27,40,41].…”

Section: Discussionmentioning

confidence: 96%

“…A common way to study carbohydrates uses lectins as probes that are known to recognize different types of oligosaccharide structures with a high affinity, comparable to that observed for antigen-antibody interactions. The known lectins' high affinity to specific sugar residues has a wide range of applications in different types of biological assays used, for example, to study the glycoprotein and carbohydrate recognition processes [23,24], to purify glycoproteins, or to characterize properties of malignant cells [25].…”

Section: Introductionmentioning

confidence: 99%

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