3 research outputs found
Ligand-Accelerated Cross-Coupling of C(sp<sup>2</sup>)–H Bonds with Arylboron Reagents
A ligand-accelerated Pd(II)-catalyzed C(sp<sup>2</sup>)–H/arylboron cross-coupling reaction of phenylacetic acid substrates is reported. Using Ac-Ile-OH as the ligand and Ag<sub>2</sub>CO<sub>3</sub> 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 O<sub>2</sub> 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<sup>–</sup> and Gram<sup>+</sup> 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<sup>–</sup> 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<sup>–</sup> and Gram<sup>+</sup> 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<sup>–</sup> 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