RESUMEN
Lectins are invaluable tools for chemical biology because they recognize carbohydrate arrays. Multivalent carbohydrate binding by lectins is important for processes such as bacterial and viral adhesion and cancer metastasis. A better understanding of mammalian lectin binding to carbohydrate arrays is critical for controlling these and other cellular recognition processes. Plant lectins are excellent model systems for the study of multivalent protein-carbohydrate interactions because of their robustness and ready availability. Here, we describe binding studies of mannose-functionalized poly(amidoamine) (PAMAM) dendrimers to a mitogenic lectin from Pisum sativum (pea lectin). Hemagglutination and precipitation assays were performed, and results were compared to those obtained from concanavalin A (Con A), a lectin that has been studied in more detail. Isothermal titration calorimetry (ITC) experiments are also described.