Carbohydrate concanavalin

T. K. Dam, R. Roy, D. Page, and C. F. Brewer, Thermodynamic binding parameters of individual epitopes of multivalent carbohydrates to concanavalin A as determined by reverse isothermal titration microcalorimetry, Biochemistry, 41 (2002) 1359-1363. 

Y. Li, X. Zhang, S. Chu, K. Yu, and H. Guan, Synthesis of cluster mannosides via a Ugi four-component reaction and their inhibition against the binding of yeast mannan to concanavalin A, Carbohydr. Res., 339 (2004) 873-879. 

J. Lehmann and U. P. Weitzel, Synthesis and application of a-D-mannosyl clusters as photoaffinity ligands for mannose-binding proteins Concanavalin A as a model receptor, Carbohydr. Res., 294 (1996) 65-94. 

M. Kohn, J. M. Benito, C. O. Mellet, T. K. Lindhorst, and J. M. Garcia Fernandez, Functional evaluation of carbohydrate-centred glycoclusters by enzyme-linked lectin assay Ligands for Concanavalin A, ChemBioChem, 5 (2004) 771-777. 

The molecular recognition of septanose carbohydrates has been investigated in depth by using concanavalin A68 as a model lectin. Complex formation was analysed by STD experiments and showed the first direct evidence of binding, by a natural protein, for this class of ring-expanded carbohydrate molecules. 

Multiple-ion monitoring is, however, of considerable value in structural studies, but only if model compounds of known structure are available for comparison. Such an approach has been used in the study of the carbohydrate structures of glycoproteins from different tissues.50 Separation of glycopeptides obtained from various tissues was performed on columns of concanavalin A-Sepharose. Structural analysis by multiple-ion monitoring of partially methylated, alditol acetates derived from the various fractions indicated that the glycopeptides were separated according to the linkage pattern of mannose (see Fig. 1). 

Taken together, these results suggest that molecular recognition of the dodecapeptide by antibodies differs from its recognition by concanavahn A, and that the immunological cross-reactivity observed in some studies does not reflect structural mimicry. That molecular recognition by concanavalin A of carbohydrates and peptides differs has also been shown in structural studies. Here, the functional molecular mimicry observed with respect to different receptors should not be assumed to imply structural mimicry—the inter-molecular interactions may differ in each case. 

Figure 13.2 The crystal structures of (a) concanavalin A and (b) the carbohydrate recognition domain of galectin-3. Residues in the carbohydrate binding sites are black.

Ramstrom O, Lehn J-M. In situ generation and screening of a dynamic combinatorial carbohydrate library against concanavalin A. ChemBioChem 2000 1 41-48. 

This fraction contained carbohydrates typical of membrane glycoproteins and was especially rich in galactose and sialic acid. Glycoproteins in this fraction avidly bound the lectin Concanavalin A. 

Ramstrom, O., Lohmann, S., Bunyapaiboonsri, T., Lehn, J.-M. Dynamic combinatorial carbohydrate libraries probing the binding site of the concanavalin A lectin. Chem. Eur. J. 2004,10, 1711-1715. 

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