Determination of 11 aminoglycosides in meat and liver by liquid chromatography with tandem mass spectrometry

A method using liquid chromatography with tandem mass spectrometry was developed for the determination of 11 commonly used aminoglycoside antibiotics in meat. The proposed method is sufficiently sensitive (detection limits of 15 to 40 ppb for the various antibiotics) and highly selective. It is suitable for the quantitation and confirmation of aminoglycosides in a variety of matrixes (pork muscle, fish, and veal liver). Any multiresidue method for aminoglycosides must take into account their high affinity toward sample proteins and the significantly different pK values of the various analytes. The developed method uses a low-pH extraction with trichloracetic acid to ensure complete extraction of the analytes from the matrix. An anion-exchange step is used to remove the acid from the centrifuged extract. Aminoglycosides in this solution of low ionic strength can be quantitatively retained and afterwards eluted from a weak cation-exchanger solid-phase extraction (SPE) cartridge. The highly selective SPE steps produce clean extracts, which minimize possible suppression of the mass spectrometer signal.     

Die Kristallstruktur von AgCu3Cu(AsO4)3 und ihre strukturellen Beziehungen zu AgCo3H2(AsO4)3 bzw. AgZn3H2(AsO4)3

Crystal Structure of AgCu₃Cu(AsO₄)₃ and its Structural Relations to AgCo₃H₂(AsO₄)₃ and AgZn₃H₂ (AsO₄)₃ The compound AgCu₃Cu(AsO₄)₃ was synthesized and investigated by X-rays. It crystallizes in the monoclinic space group C2/c with a = 1 212.7(2), b = 1 249.0(2), c = 727.8(1) pm, β = 117.94(1)°, Z = 4. The structure is closely related to the structures of AgCo₃H₂(AsO₄)₃ and AgZn₃H₂(AsO₄)₃. Only two hydrogen atoms are replaced by an additional copper atom forming a copper coordination square instead of two hydrogen bridges. The remaining copper atoms are sixfold coordinated with the generally observed Jahn-Teller distortion. Whereas in AgCo₃H₂(AsO₄)₃ and AgZn₃H₂(AsO₄)₃ silver has a (4+4) coordination, it is in this compound distinctly eightfold coordinated.     

Über P–P-haltige cyclische Verbindungen. II

On P? P Containing Cyclic Compounds. II. Reaction of N,N'-dimethylthiourea with phenyl dichlorophosphane yields 1.4-dimethyl-2. 3-diphenyl-1.4.2.3-diazadiphospholidine-5-thione-2-sulfide ( II ). The compound is characterized by its nmr, vibration and mass spectra as well as the results of an X-ray structural analysis. Byproduct of the reaction is N-(N,N'-dimethylcarbamimidoyl)-N,N'-dimethyl thiourea hydrochloride ( III ), which crystallizes with pyridinium chloride. Molecular and crystal structure are reported. With methyl dichlorophosphane N,N'-dimethylthiourea forms 1.2.3.4-tetramethyl-1.4.2.3-diazadiphospholidine-5-thione-2-sulfide ( IV ), which is characterized by its nmr and vibration spectra.     

Analysis of spin states, spin barriers, and trans-effects involved in the coordination and stabilization of dinitrogen by biomimetic iron complexes

Coordination of dinitrogen to Sellmann-type iron (II) complexes in a sulfur-dominated coordination sphere, which emulates the environment of iron centers in the FeMo-cofactor of nitrogenase, is analyzed with respect to spin states, spin barriers, and the effect of trans-ligands. Such detailed investigations became only recently feasible when the reliability of density functional methods, which are the only quantum chemical methods capable of describing large transition metal complexes, could significantly be improved for the calculation of energies for states of different spin. It is found that the actual binding energy of dinitrogen is of sufficient magnitude for a reasonably strong fixation of N₂ by Sellmann-type coordination compounds. However, potential fixation is determined by additional factors which reduce the binding energy. One factor is the change in spin state of the N₂-free metal fragment, which lowers the total energy and quenches the thermodynamic stabilization effect of the binding energy. In addition, the metal fragment rearranges and gains even more stabilization energy for the un-coordinated state. Apart from these thermodynamical effects, the existence of spin barriers, which must be overcome upon binding of dinitrogen, leads to kinetical effects, which cannot be neglected.     

Optimization of auxiliary basis sets for the LEDO expansion and a projection technique for LEDO-DFT

We present a systematic procedure for the optimization of the expansion basis for the limited expansion of diatomic overlap density functional theory (LEDO-DFT) and report on optimized auxiliary orbitals for the Ahlrichs split valence plus polarization basis set (SVP) for the elements H, Li--F, and Na--Cl. A new method to deal with near-linear dependences in the LEDO expansion basis is introduced, which greatly reduces the computational effort of LEDO-DFT calculations. Numerical results for a test set of small molecules demonstrate the accuracy of electronic energies, structural parameters, dipole moments, and harmonic frequencies. For larger molecular systems the numerical errors introduced by the LEDO approximation can lead to an uncontrollable behavior of the self-consistent field (SCF) process. A projection technique suggested by L?wdin is presented in the framework of LEDO-DFT, which guarantees for SCF convergence. Numerical results on some critical test molecules suggest the general applicability of the auxiliary orbitals presented in combination with this projection technique. Timing results indicate that LEDO-DFT is competitive with conventional density fitting methods.     

Prerequisites for peptidomic analysis of blood samples: II. Analysis of human plasma after oral glucose challenge -- a proof of concept

Mass spectrometric plasma analysis for biomarker discovery has become an exploratory focus in proteomic research: the challenges of analyzing plasma samples by mass spectrometry have become apparent not only since the human proteome organization (HUPO) has put much emphasis on the human plasma proteome. This work demonstrates fundamental proteomic research to reveal sensitivity and quantification capabilities of our Peptidomics technologies by detecting distinct changes in plasma peptide composition in samples after challenging healthy volunteers with orally administered glucose. Differential Peptide Display (DPD) is a technique for peptidomics studies to compare peptides from distinct biological samples. Mass spectrometry (MS) is used as a qualitative and quantitative analysis tool without previous trypsin digestion or labeling of the samples. Circulating peptides (< 15 kDa) were extracted from 1.3 mL plasma samples and the extracts separated by liquid chromatography into 96 fractions. Each fraction was subjected to MALDI MS, and mass spectra of all fractions were combined resulting in a 2D-display of > 2,000 peptides from each sample. Endogenous peptides that responded to oral glucose challenge were detected by DPD of pre-and post-challenge plasma samples from 16 healthy volunteers and subsequently identified by nESI-qTOF MS. Two of the 15 MS peaks that were significantly modulated by glucose challenge were subsequently identified as insulin and C-peptide. These results were validated by using immunoassays for insulin and C-peptide. This paper serves as a proof of principle for proteomic biomarker discovery down to the pM concentration range by using small amounts of human plasma.