857677-98-6Relevant articles and documents
Synthesis of a novel fluorescent ruthenium complex with an appended Ac4GlcNAc moiety by click reaction
Cheng, Qi,Cui, Yalu,Xiao, Nao,Lu, Jishun,Fang, Chen-Jie
, p. 1 - 10 (2018/07/31)
The O-linked β-N-acetylglucosamine (O-GlcNAc) modification is an abundant post-translational modification in eukaryotic cells, which plays a fundamental role in the activity of many cells and is associated with pathologies like type II diabetes, Alzheimer’s disease or some cancers. However, the precise connexion between O-GlcNAc-modified proteins and their function in cells is largely undefined for most cases. Confocal microscopy is a powerful and effective tool for in-cell elucidation of the function of biological molecules. Chemical labeling of non-ultraviolet or non-fluorescent carbohydrates with fluorescent tag is an essential step that makes intra-cellular microscopic inspection possible. Here we report a strategy based on the 1,3-dipolar cycloaddition, called click chemistry, between unnatural N-acetylglucosamine (GlcNAc) analogues Ac4GlcNAc (substituted with an azido group) and the corresponding fluorescent tag Ru(bpy)2(Phen-alkyne)Cl2 (4) to synthesize the fluorescent dye Ru(bpy)2(Phen-Ac4GlcNAc)Cl2 (5) under mild and neutral reaction conditions. Moreover, 5 showed good stability, desirable fluorescence characteristics, and exhibited rather low levels of cytotoxicity against sensitive MCF-7 cells. Additionally, we have achieved successful fluorescent imaging of 5 transported in living MCF-7 cells. Cell images displayed that proteins are potentially labelled with 5 in the cytoplasm.
Glucosamine- and galactosamine- based monosaccharides with highly fluorinated motifs
Tomaszewska, Joanna,Kowalska, Karolina,Koroniak-Szejn, Katarzyna
, p. 1 - 13 (2016/09/23)
Synthesis of modified monosaccharides, derivatives of glucose and galactose, having a highly fluorinated chain, as a library of synthetic building blocks for hyaluronic acid (HA) modified subunits has been developed. “Click” chemistry has been employed as a strategy for the synthesis of these molecules. 1,2,3-triazole ring derivatives were obtained with good to excellent yields.
O-GlcNAc peptide epoxyketones are recognized by mammalian proteasomes
Witte, Martin D.,Florea, Bogdan I.,Verdoes, Martijn,Adeyanju, Oloruntosin,Van Der Marel, Gijs A.,Overkleeft, Herman S.
supporting information; experimental part, p. 12064 - 12065 (2010/01/30)
(Chemical Equation Presented) Cytosolic and nuclear proteins may be subject to both O-GlcNAcylation and proteasomal degradation. By means of activity-based profiling, we demonstrate that O-GlcNAc serinecontaining peptide epoxyketones bind to the proteasome catalytic active sites and thus provide the first clear evidence that proteasomes recognize peptides post-translationally modified with a GlcNAc moiety.
