In Situ Fluorescence Imaging of the Levels of Glycosylation and Phosphorylation by a MOF-Based Nanoprobe in Depressed Mice

Elucidating the relationship between glycosylation and phosphorylation of protein post-translational modifications is of great significance for understanding most diseases. Mass spectrometry has been widely used in research of protein phosphorylation and glycosylation. However, to realize in situ and dynamic analysis of the levels of phosphorylation and glycosylation in cells and in vivo, mass spectrometry still has certain difficulties. Herein, a nano-MOF-based fluorescent probe with Zr(IV) and boric acid as the active center was designed and prepared. Fluorescence detection and imaging of phosphate is achieved through the specific interaction of Zr(IV) and phosphate. With aim to achieve specific recognition of glycosylation sites, the boronic acid group was modified in the MOF structure, and the fluorescence of the MOFs was regulated by the alizarin red. Thus, the glycosylation sites were recognized by the competition between alizarin red and glycosyl. Finally, the nanoprobe was successfully applied for in situ fluorescence imaging of the levels of glycosylation and phosphorylation in depressed mice.