Photoproximity Labeling from Single Catalyst Sites Allows Calibration and Increased Resolution for Carbene Labeling of Protein Partners In Vitro and on Cells.

The cell surface proteome (surfaceome) plays a pivotal role in virtually all extracellular biology, and yet we are only beginning to understand the protein complexes formed in this crowded environment. Recently, a high-resolution approach (μMap) was described that utilizes multiple iridium-photocatalysts attached to a secondary antibody, directed to a primary antibody of a protein of interest, to identify proximal neighbors by light-activated conversion of a biotin-diazirine to a highly reactive carbene followed by LC/MS (Geri, J. B.

Roadmap for Optimizing and Broadening Antibody-Based PROTACs for Degradation of Cell Surface Proteins.

Targeted protein degradation is a promising therapeutic strategy capable of overcoming the limitations of traditional occupancy-based inhibitors. By ablating all of the associated functions of a protein at once, the event-driven pharmacology of degrader technologies has recently enabled the targeting of proteins that have been historically deemed "undruggable". Most degradation strategies utilize the ubiquitin-proteasome system to mediate intracellular target degradation and are thus limited to targeting proteins with cytoplasmic domains.

Heterogenized Pyridine-Substituted Cobalt(II) Phthalocyanine Yields Reduction of CO by Tuning the Electron Affinity of the Co Center.

Conversion of CO to reduced products is a promising route to alleviate irreversible climate change. Here we report the synthesis of a Co-based phthalocyanine with pyridine moieties (CoPc-Pyr), which is supported on a carbon electrode and shows Faradaic efficiency ∼90% for CO at 490 mV of overpotential (-0.6 V vs reversible hydrogen electrode (RHE)).