title: Mannose/glucose-functionalized dendrimers to investigate the predictable tunability of multivalent interactions.
abstract: 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.
authors.affiliation: Department of Chemistry and Biochemistry and Center for Bioinspired Nanomaterials, Montana State University, 108 Gaines Hall, Bozeman, Montana 59717, USA.
authors.forename: Mark L
authors.initials: ML
authors.lastname: Wolfenden
authors.forename: Mary J
authors.initials: MJ
authors.lastname: Cloninger
mesh_terms: D001665:Binding Sites; D002241:Carbohydrates / Q000138:chemical synthesis; D005947:Glucose / Q000737:chemistry*; D017879:Isothiocyanates / Q000737:chemistry; D046911:Macromolecular Substances / Q000737:chemistry*; D008358:Mannose / Q000737:chemistry*; D008956:Models, Chemical; D011506:Proteins / Q000737:chemistry*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D002241:Carbohydrates; D017879:Isothiocyanates; D046911:Macromolecular Substances; D011506:Proteins; D005947:Glucose; D008358:Mannose