Description
Small molecules selectively interacting with proteins and thereby modulating enzyme activity are of great interest for chemical biology and chemical medicine. Altering the intrinsic catalytic activity, either through enzyme activation or inhibition, leads to decisive effects on the biological system [1].With the development of activity-based protein profiling (ABPP), detection of actually active enzyme rather than the expression level of the protein became feasible. Furthermore, ABPP has been used for the identification of new drug targets and has highly accelerated the process of drug development [2].
In a variation of ABPP termed ligand-directed chemistry (LDC), profiling of enzymes without losing their intrinsic activity was achieved [3]. In this approach, the small molecule probe is equipped with a reversible inhibitor as ligand (A) and a cleavable electrophilic reactive group (B) for covalent bond formation, nearby, but outside the active site (Figure 1).
Here we present the design, synthesis and biological evaluation of iminosugar based probes for selective profiling of glycoside hydrolases, applying the ligand-directed chemistry (LDC) approach. Experimental details and results of the biological activity of our probes will be presented.
| Period | 9 Jul 2023 → 13 Jul 2023 |
|---|---|
| Event title | The 21st European Carbohydrate Symposium in Paris |
| Event type | Conference |
| Conference number | 21 |
| Location | Paris, FranceShow on map |
| Degree of Recognition | International |