Altering the Strength of Lectin Binding Interactions and Controlling the Amount of Lectin Clustering Using Mannose/Hydroxyl-Functionalized Dendrimers

Citations Over TimeTop 10% of 2003 papers

Abstract

Protein-carbohydrate interactions play a critical role in many biological recognition events. Multivalent therapeutic agents that utilize protein-carbohydrate interactions have proven difficult to design, primarily because the fundamental requirements of protein-carbohydrate interactions are not well understood. Here, we report a systematic study of the effect on lectin binding of varying the loading of mannose surface residues on generations three through six PAMAM dendrimers. The degree of mannose functionalization was controlled by stoichiometric addition, and dendrimers were characterized using NMR and MALDI-TOF MS. Hemagglutination assays and quantitative precipitation assays were performed to determine the relative activity of the dendrimers. Using the mannose/hydroxyl-functionalized dendrimers reported here, we could systematically control both the degree of lectin clustering and the overall activity of the lectin with the dendrimer.

Related Papers

• Dendrimers in medicine and biotechnology. New molecular tools(2006)
• → Force Biased Molecular Dynamics Simulation Study of Effect of Dendrimer Generation on Interaction with DNA(2012)25 cited
• → Near-planar Solution Structures of Mannose-binding Lectin Oligomers Provide Insight on Activation of Lectin Pathway of Complement(2011)28 cited
• → A novel measurement method for activation of the lectin complement pathway via both mannose-binding lectin (MBL) and L-ficolin(2009)8 cited
• → A Lectin from Leaves of Neoregelia flandria Recognizes D-Glucose, D-Mannose and N-Acetyl D-glucosamine, Differing from the Mannose-Specific Lectins of Other Monocotyledonous Plants(1996)10 cited