Mannose/Glucose-Functionalized Dendrimers To Investigate the Predictable Tunability of Multivalent Interactions

• Published in: Journal of the American Chemical Society Vol. 127; no. 35; pp. 12168 - 12169
• Main Authors: Wolfenden, Mark L, Cloninger, Mary J
• Format: Journal Article
• Language: English
• Published: WASHINGTON American Chemical Society 07.09.2005; Amer Chemical Soc
• Subjects: Binding Sites; Biological and medical sciences; Carbohydrates - chemical synthesis; Chemistry; Chemistry, Multidisciplinary; Fundamental and applied biological sciences. Psychology; Glucose - chemistry; Interactions. Associations; Intermolecular phenomena; Isothiocyanates - chemistry; Macromolecular Substances - chemistry; Mannose - chemistry; Models, Chemical; Molecular biophysics; Physical Sciences; Proteins - chemistry; Science & Technology; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; CONCANAVALIN-A; LECTIN; THERMODYNAMICS; BINDING; Hemagglutination; Functionalization; Chemical affinity; Molecular association; Molecular interaction; Mannose; Allylic amine polymer; Glucose; Concanavalin A; Dendritic structure
• ISSN: 0002-7863; 1520-5126
• DOI: 10.1021/ja053008n

G4-, G5-, and G6-PAMAM dendrimers were functionalized with mixtures of mannose and glucose in varying ratios, and the relative affinities of these compounds for Concanavalin A (Con A) were evaluated using the hemagglutination assay. As the ratio of mannose to glucose increases, the relative activity in the hemagglutination assay (on a per sugar basis) increases linearly. Methyl mannose binds to Con A with an affinity 4-fold higher than that of methyl glucose; multivalency amplifies this trend. The mannose/glucose-functionalized dendrimer results reported here suggest that the affinity of multivalent associations can be attenuated in predictable, reliable ways based on monovalent affinities of the ligands.