917222-23-2Relevant academic research and scientific papers
Synthetic Glycosphingolipids for Live-Cell Labeling
Dauner, Martin,Batroff, Ellen,Bachmann, Verena,Hauck, Christof R.,Wittmann, Valentin
, p. 1624 - 1637 (2016)
Glycosphingolipids are an important component of cell membranes that are involved in many biological processes. Fluorescently labeled glycosphingolipids are frequently used to gain insight into their localization. However, the attachment of a fluorophore to the glycan part or - more commonly - to the lipid part of glycosphingolipids is known to alter the biophysical properties and can perturb the biological function of the probe. Presented here is the synthesis of novel glycosphingolipid probes with mono- and disaccharide head groups and ceramide moieties containing fatty acids of varying chain length (C4 to C20). These glycosphingolipids bear an azide or an alkyne group as chemical reporter to which a fluorophore can be attached through a bioorthogonal ligation reaction. The fluorescent tag and any linker connected to it can be chosen in a flexible manner. We demonstrate the suitability of the probes by selective visualization of the plasma membrane of living cells by confocal microscopy techniques. Whereas the derivatives with the shorter fatty acids can be directly applied to HEK 293T cells, the hydrophobic glycosphingolipids with longer fatty acids can be delivered to cells using fusogenic liposomes.
Activity-based protein profiling reagents for protein arginine deiminase 4 (PAD4): Synthesis and in vitro evaluation of a fluorescently labeled probe
Luo, Yuan,Knuckley, Bryan,Bhatia, Monica,Pellechia, Perry J.,Thompson, Paul R.
, p. 14468 - 14469 (2006)
Protein arginine deiminase 4 (PAD4), which catalyzes the post-translational conversion of peptidyl arginine to peptidyl citrulline, is widely regarded as one of the best new targets for the development of a novel rheumatoid arthritis therapeutic. In addition to its presumed role in this disease, PAD4 is also a calcium-dependent histone deiminase that acts as a transcriptional co-repressor. Herein we describe the design, synthesis, and in vitro evaluation of two fluorescently labeled activity-based protein profiling (ABPP) reagents that specifically and irreversibly modify the active, that is, calcium-bound, form PAD4 with equal affinity to previously described small molecule chemical probes of PAD4 function. These fluorescently tagged ABPPs will be useful for identifying the conditions under which this enzyme is activated in vivo and may prove to be useful RA diagnostics. Copyright
SYNTHESIS AND USE OF NOVEL INHIBITORS AND INACTIVATORS OF PROTEIN ARGININE DEIMINASES
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Page/Page column 32-33, (2008/06/13)
In one embodiment of the present disclosure, an inactivator of protein arginine deiminase 4 is disclosed. The inactivator includes: (I) and x includes F, Cl, and H, y includes OH and NH2, R includes H, an alkyl group, an alkenyl group, an alknyl group, and n is greater than 0.
