Altering the strength of lectin binding interactions and controlling the amount of lectin clustering using mannose/hydroxyl-functionalized dendrimers
| Autor: | Eric K. Woller, Eric D. Walter, Mary J. Cloninger, David J. Singel, Joel R. Morgan |
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| Rok vydání: | 2003 |
| Předmět: |
Dendrimers
Magnetic Resonance Spectroscopy biology Mannose Lectin General Chemistry Nuclear magnetic resonance spectroscopy Carbohydrate Biochemistry Catalysis chemistry.chemical_compound Matrix-assisted laser desorption/ionization Colloid and Surface Chemistry Molecular recognition chemistry Dendrimer Lectins Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization biology.protein Concanavalin A Polyamines Surface modification |
| Zdroj: | Journal of the American Chemical Society. 125(29) |
| ISSN: | 0002-7863 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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