Dependence of Concanavalin A Binding on Anomeric Configuration, Linkage Type, and Ligand Multiplicity for Thiourea-Bridged Mannopyranosyl–β-Cyclodextrin Conjugates
✍ Scribed by Isabelle Baussanne; Juan Manuel Benito; Carmen Ortiz Mellet; José Manuel García Fernández; Jacques Defaye
- Publisher
- John Wiley and Sons
- Year
- 2001
- Tongue
- English
- Weight
- 143 KB
- Volume
- 2
- Category
- Article
- ISSN
- 1439-4227
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✦ Synopsis
Concanavalin A (Con A), the mannose-specific lectin from Concanavalia ensiformis, has long been used as a model for carbohydrate ± protein interactions. [1] Its commercial availability and the rather extensive structural knowledge currently available make it attractive for assessing and optimizing the functional parameters that affect its affinity for mannose neoglycoconjugates. Understanding these key elements may facilitate the development of new therapeutic strategies based on specific recognition events such as targeting of drugs.
Con A binds a-D-mannopyranosides preferentially over the corresponding b anomers. [2] The affinity for monosaccharide ligands is low; however, this is a rather common feature when considering protein ± carbohydrate interactions. Carbohydrate ± protein binding events usually involve several simultaneous contacts between carbohydrates that are clustered on cell surfaces and protein receptors that contain multiple carbohydrate-binding sites. Based on this concept, one could anticipate that multiplication of the saccharide epitope on the surface of the carrier may lead to a greater affinity than predicted from the sum of the constitutive one-to-one interactions [3, 4] Ðthe so-