Targeted mass spectrometry (MS) approaches, which are powerful methods for uniquely and confidently quantifying a specific panel of proteins in complex biological samples, play a crucial role in validating and clinically translating protein biomarkers discovered through global proteomic profiling. Common targeted MS methods, such as multiple reaction monitoring (MRM) and parallel-reaction monitoring (PRM), employ specific mass spectrometric technologies to quantify protein levels by comparing the transitions of surrogate endogenous (ENDO) peptides with those of stable isotope-labeled (SIL) peptide counterparts. These methods utilizing amino acid analyzed (AAA) SIL peptides warrant sensitive and precise measurements required for targeted MS assays.
View Article and Find Full Text PDFProteomics has played a central role in the identification of reliable disease biomarkers, which are the basis of precision medicine, a promising approach for tackling recalcitrant diseases such as cancer, that elude conventional treatments. Among proteomic methodologies, targeted proteomics employing stable isotope-labeled (SIL) internal standards is particularly suited for the clinical translation of biomarker information owing to its high throughput and accuracy in the quantitative analysis of patient-derived proteomes. Using SIL internal standards ensures the utmost level of confidence in detection and precision in targeted MS experiments.
View Article and Find Full Text PDFA new nickel(II) porphyrin complex, [Ni (porp)] (1), has been synthesized and characterized by H NMR, C NMR and mass spectrometry analysis. This Ni porphyrin complex 1 quantitatively catalyzed the epoxidation reaction of a wide range of olefins with meta-chloroperoxybenzoic acid (m-CPBA) under mild conditions. Reactivity and Hammett studies, H O-exchange experiments, and the use of PPAA (peroxyphenylacetic acid) as a mechanistic probe suggested that participation of multiple active oxidants Ni -OOC(O)R 2, Ni -Oxo 3, and Ni -Oxo 4 within olefin epoxidation reactions by the nickel porphyrin complex is markedly affected by solvent polarity, concentration, and type of substrate.
View Article and Find Full Text PDFDinuclear Fe and Ni complexes, [(phenO)Fe(N )] (NO ) (1) and [(phenOH)Ni(N ) ] (2), were prepared by treating Fe(NO ) ⋅9 H O and Ni(NO ) ⋅6 H O in methanol, respectively, with phenOH (=N-(2-pyridylmethyl)-N'-(2-hydroxyethyl)ethylenediamine) and NaN ; both 1 and 2 were characterized by elemental analysis, IR spectroscopy, X-ray diffraction, and magnetic susceptibility measurements. Two ethoxo-bridged Fe and two azido-bridged Ni were observed in 1 and 2, respectively; corresponding antiferromagnetic interaction via the bridged ethoxo groups and strong ferromagnetic coupling via the bridged end-on azido ligands within the dimeric unit were observed. Complex 1 did not exhibit any catalytic activity, while 2 exhibited excellent catalytic activities for the epoxidation of aliphatic, aromatic, and terminal olefins.
View Article and Find Full Text PDFA new mononuclear nickel(II) complex, [Ni (dpaq)Cl] (1), containing a tetradentate monoamido ligand, dpaq (dpaq=2-[bis(pyridin-2-ylmethyl)amino]-N-(quinolin-8-yl)acetamide), has been synthesized and characterized by IR spectroscopy, elemental analysis, and UV/Vis spectroscopy. The structure of the nickel complex has been determined by X-ray crystallography. This nonheme Ni complex 1 catalyzed the epoxidation reaction of a wide range of olefins with meta-chloroperoxybenzoic acid (m-CPBA) under mild conditions.
View Article and Find Full Text PDFA new colorimetric and fluorescent receptor 1 for the detection of CN(-) has been simply developed. Receptor 1 showed selectively colorimetric and fluorometric responses to CN(-) in a near-perfect aqueous solution, respectively. This sensor displayed an obvious color change from yellow to colorless upon selective binding with CN(-).
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