125770-90-3Relevant academic research and scientific papers
Targeted mass spectrometry-based approach for protein-ligand binding analyses in complex biological mixtures using a phenacyl bromide modification strategy
Jin, Lorrain,Wang, Dongyu,Gooden, David M.,Ball, Carol H.,Fitzgerald, Michael C.
, p. 10987 - 10993 (2016)
The characterization of protein folding stability changes on the proteomic scale is useful for protein-target discovery and for the characterization of biological states. The Stability of Proteins from Rates of Oxidation (SPROX) technique is one of several mass spectrometry-based techniques recently established for the making proteome-wide measurements of protein folding and stability. A critical part of proteome-wide applications of SPROX is the identification and quantitation of methionine-containing peptides. Demonstrated here is a targeted mass spectrometrybased proteomics strategy for the detection and quantitation of methionine-containing peptides in SPROX experiments. The strategy involves the use of phenacyl bromide (PAB) for the targeted detection and quantitation of methionine-containing peptides in SPROX using selective reaction monitoring (SRM) on a triple quadrupole mass spectrometer (QQQ-MS). As proof-of-principle, the known binding interaction of Cyclosporine A with cyclophilin A protein in a yeast cell lysate is successfully detected and quantified using a targeted SRM workflow. Advantages of the described workflow over other SPROX protocols include a 20-fold reduction in the amount of total protein needed for analysis and the ability to work with the endogenous proteins in a given sample (e.g., stabile isotope labeling with amino acids in cell culture is not necessary).
Synthesis of 14C-labeled levamisole and 13C-labeled tetramisole
Feil
, p. 1071 - 1076 (2007/10/03)
The syntheses of 14C-ring labeled levamisole ([-]-2,3.5,6-tetrahydro-6-phenyl[14C-UL)imidazo[2,1- b]thiazole) from acetophenone-ring-UL-14C in 5 steps plus resolution with a 7.5% overall yield, and 13C6/su
