Bifurcation of Excited-State Population Leads to Anti-Kasha Luminescence in a Disulfide-Decorated Organometallic Rhenium Photosensitizer.

We report a rhenium diimine photosensitizer equipped with a peripheral disulfide unit on one of the bipyridine ligands, [Re(CO)(bpy)(bpy)] (, bpy = 2,2'-bipyridine, bpy = [1,2]dithiino[3,4-:6,5-']dipyridine), showing anti-Kasha luminescence. Steady-state and ultrafast time-resolved spectroscopies complemented by nonadiabatic dynamics simulations are used to disclose its excited-state dynamics. The calculations show that after intersystem crossing the complex evolves to two different triplet minima: a (bpy)-ligand-centered excited state (LC) lying at lower energy and a metal-to-(bpy)-ligand charge transfer (MLCT) state at higher energy, with relative yields of 90% and 10%, respectively.

Profiling the interactome of oligonucleotide drugs by proximity biotinylation.

Drug-ID is a novel method applying proximity biotinylation to identify drug-protein interactions inside living cells. The covalent conjugation of a drug with a biotin ligase enables targeted biotinylation and identification of the drug-bound proteome. We established Drug-ID for two small-molecule drugs, JQ1 and SAHA, and applied it for RNaseH-recruiting antisense oligonucleotides (ASOs).

Extending the enzymatic toolbox for heparosan polymerization, depolymerization, and detection.

Heparosan is an acidic polysaccharide expressed as a capsule polymer by pathogenic and commensal bacteria, e.g. by E.

Peptide CoA conjugates for in situ proteomics profiling of acetyltransferase activities.

The acetylation of protein N-termini is a co- or posttranslational modification that plays important roles in protein homeostasis and stability. N-terminal acetyltransferases (NATs) catalyze the introduction of this modification using acetyl-coenzyme A (acetyl-CoA) as source of the acetyl-group. NATs operate in complex with auxiliary proteins that impact activity and specificity of these enzymes.