Photoactivatable O-GlcNAc Transferase Library Enables Covalent Chemical Capture of Solvent-Exposed TPR Domain Interactions.

O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT) is an essential, stress-sensing enzyme responsible for adding the O-GlcNAc monosaccharide to thousands of nuclear and cytoplasmic proteins to regulate cellular homeostasis. OGT substrates are found in almost all intracellular processes, and perturbations in protein O-GlcNAc levels have been implicated in proteostatic diseases, such as cancers, metabolic disorders, and neurodegeneration. This broad disease activity makes OGT an attractive therapeutic target; however, the substrate diversity makes pan-inhibition as a therapeutic strategy unfeasible.

Synthesis of P-triazole dithienophospholes and a cyclodextrin-based sensor via click chemistry.

The synthesis of a series of highly luminescent, functional dithienophospholes via a click reaction is reported. Slight modification of the lateral aromatic substituents leads to a significant difference in their solid-state organization. In addition, a novel water-soluble β-cyclodextrin hybrid is demonstrated to be an effective sensor for picric acid.

Halochromic generation of white light emission using a single dithienophosphole luminophore.

A new dithienophosphole-based donor-acceptor conjugated luminophore shows a large halochromic effect on its emission color that changes from red to green upon addition of acid. White light emission can be generated upon partial protonation resulting in a broad emission band.