Cyclodextrin-functionalized chromatographic materials tailored for reversible adsorption.

Novel dendronized silica substrates were synthesized. First- and second- generation polyaryl ether dendrons were appended to silica surfaces. Using Cu(I) mediated cycloaddition "click" chemistry, β-cyclodextrin was tethered to the dendronized surfaces and to a nondendronized surface for comparison purposes.

Clusters of ligands on dendrimer surfaces.

The development of methodology that is designed to allow a significant increase in the patterning and in the functionalization of the dendrimer is the ultimate goal of the research described here. Glycoside clusters based on TRIS were formed using click chemistry and were attached to PAMAM dendrimers. A series of dendrimers bearing tris-mannoside and an ethoxyethanol group was synthesized, and the binding interactions of these dendrimers with Concanavalin A were evaluated using inhibition ELISAs.

Inhibition binding studies of glycodendrimer-lectin interactions using surface plasmon resonance.

Understanding protein-carbohydrate interactions is essential for elucidating biological pathways and cellular mechanisms but is often difficult due to the prevalence of multivalent interactions. Here, we evaluate the multivalent glycodendrimer framework as a means to describe the inhibition potency of multivalent mannose-functionalized dendrimers using surface plasmon resonance (SPR). Using highly robust, mannose-functionalized dithiol self-assembled monolayers on gold surfaces, we found that glycodendrimers were efficient inhibitors of protein-carbohydrate interactions.

Characterization of protein aggregation via intrinsic fluorescence lifetime.

Aggregation plays an integral role in multivalent protein-carbohydrate interactions, Alzheimer's and other amyloid-related diseases, and infection response. Efforts to apply controlled aggregation in toxin sensors have been made. We have developed a label-free intrinsic fluorescence lifetime assay that uniquely can monitor aggregation processes in real time without interference from precipitation.

Binding of mannose-functionalized dendrimers with pea (Pisum sativum) lectin.

Lectins are invaluable tools for chemical biology because they recognize carbohydrate arrays. Multivalent carbohydrate binding by lectins is important for processes such as bacterial and viral adhesion and cancer metastasis. A better understanding of mammalian lectin binding to carbohydrate arrays is critical for controlling these and other cellular recognition processes.