Peanut lectin carbohydrate-binding specificity

Polymer adsorption has also been adapted to QCM sensing whereby biofunctional thin films are adsorbed on the crystal surface with non-specific binding controlled by tuning of polymer composition. This approach proved successful as applied to carbohydrate-protein interaction by Matsuura et al. through adsorption of lactose bearing amphiphilic polymers on hydrophobic surfaces which then showed RCA12o and peanut lectin (PNA) affinity [33]. Carbohydrate surfaces prepared by photo insertion into an adsorbed polymer were tested by QCM and showed the predicted affinities [34] while in another example a covalently bound glycopolymer demonstrated Concanavalin A detection ability [35]. 

Besides these three major protein classes, plant lectins, also known as plant agglutinins, were shown to react with the carbohydrate moieties of IgE, inducing histamine release and thus causing allergy-like symptoms [42,43]. One 31 kDa peanut agglutinin was already identified as a lectin binding specifically to the IgE epitope [44]. 

Carbohydrate chains of Cl-inhibitor were identified by a binding assay using different lectins [36]. Lectins from Sambucus nigra (SNA) and Maackia amurensis (MAA), that are specific for sialic acids, were shown to bind to Cl-inhibitor. Lectin from Datura stramonium (DSA) also reacted with the inhibitor indicating complex and hybrid sugar structures. Cl-inhibitor was enzymatically desialylated and reexamined for lectin binding. SNA and MAA did not react anymore, but in addition to DSA, peanut agglutinin, which can bind to carbohydrate chains after sialic acids are removed, bound to desialylated Cl-inhibitor. Cl-inhibitor contains about 30 sialic acid residues per molecule. SDS-... 

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