Semisynthetic lectin-4-dimethylaminopyridine conjugates for labeling and profiling glycoproteins on live cell surfaces.

Glycoproteins on cell surfaces play important roles in biological processes, including cell-cell interaction/signaling, immune response, and cell differentiation. Given the diversity of the structure of glycans, labeling and imaging of selected glycoproteins are challenging, although several promising strategies have been developed recently. Here, we design and construct semisynthetic reactive lectins (sugar-binding proteins) that are able to selectively label glycoproteins.

Construction of a 19F-lectin biosensor for glycoprotein imaging by using affinity-guided DMAP chemistry.

In this study, assisted by affinity-guided DMAP strategy, we developed a novel (19)F-modified lectin as a biosensor for specific detection and imaging of glycoproteins. Exploited the large chemical shift anisotropy property of (19)F nuclei, glycoproteins detected by our (19)F-biosensor are signatured by broadened peaks in (19)F NMR, hence enabled the distinction between glycoproteins and small molecule saccharides. Such signal on/off switching was also applied to glycoprotein imaging by (19)F MRI.

Synthesis of scyllo-inositol derivatives and their effects on amyloid beta peptide aggregation.

scyllo-Inositol has shown promise as a potential therapeutic for Alzheimer's disease, by directly interacting with the amyloid beta (Abeta) peptide to inhibit Abeta42 fiber formation. To explore the molecular details of the inositol-Abeta42 interaction, a series of scyllo-inositol derivatives have been synthesized which contain deoxy, fluoro, chloro, and methoxy substitutions. The effects of these compounds on the aggregation cascade of Abeta42 have been investigated using electron microscopy (EM).