Ligand-Accelerated Cross-Coupling of C(sp²)–H Bonds with Arylboron Reagents

A ligand-accelerated Pd(II)-catalyzed C(sp²)–H/arylboron cross-coupling reaction of phenylacetic acid substrates is reported. Using Ac-Ile-OH as the ligand and Ag₂CO₃ as the oxidant, a fast, high-yielding, operationally simple, and functional group-tolerant protocol has been developed for the cross-coupling of phenylacetic acid substrates with aryltrifluoroborates. This ligand scaffold has also been shown to improve catalysis using 1 atm O₂ as the sole reoxidant, which sheds light on the path forward in developing optimized ligands for aerobic C–H/arylboron cross-coupling

Triflic Acid Treatment Enables LC-MS/MS Analysis of Insoluble Bacterial Biomass

The lysis and extraction of soluble bacterial proteins from cells is a common practice for proteomics analyses, but insoluble bacterial biomasses are often left behind. Here, we show that with triflic acid treatment, the insoluble bacterial biomass of Gram^– and Gram⁺ bacteria can be rendered soluble. We use LC-MS/MS shotgun proteomics to show that bacterial proteins in the soluble and insoluble postlysis fractions differ significantly. Additionally, in the case of Gram^– Pseudomonas aeruginosa, triflic acid treatment enables the enrichment of cell-envelope-associated proteins. Finally, we apply triflic acid to a human microbiome sample to show that this treatment is robust and enables the identification of a new, complementary subset of proteins from a complex microbial mixture

Triflic Acid Treatment Enables LC-MS/MS Analysis of Insoluble Bacterial Biomass

The lysis and extraction of soluble bacterial proteins from cells is a common practice for proteomics analyses, but insoluble bacterial biomasses are often left behind. Here, we show that with triflic acid treatment, the insoluble bacterial biomass of Gram^– and Gram⁺ bacteria can be rendered soluble. We use LC-MS/MS shotgun proteomics to show that bacterial proteins in the soluble and insoluble postlysis fractions differ significantly. Additionally, in the case of Gram^– Pseudomonas aeruginosa, triflic acid treatment enables the enrichment of cell-envelope-associated proteins. Finally, we apply triflic acid to a human microbiome sample to show that this treatment is robust and enables the identification of a new, complementary subset of proteins from a complex microbial mixture