AI Article Synopsis
- Protein-carbohydrate interactions are essential for many biological recognition processes, but designing multivalent therapeutic agents using these interactions is challenging due to a lack of understanding.
- A study was conducted to investigate how varying the amount of mannose on PAMAM dendrimers affects their binding to lectins, with dendrimers characterized through NMR and MALDI-TOF MS.
- Results showed that by modifying mannose levels on the dendrimers, researchers could effectively control lectin clustering and overall activity.
Article 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.
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