Sodium salts of cyclodextrins are commonly used in capillary electrophoresis/mass spectrometry (CE/MS) analysis of illicit drugs and their optical isomers. To avoid the suppression effect of cyclodextrins under electrospray ionization (ESI), the partial filling technique (PFT) is commonly utilized, which has a limited resolution. Low-flow nano-ESI has been shown to reduce the suppression effect of the salts. To test the compatibility of low-flow ESI with a background electrolyte (BGE) containing sodium salts of cyclodextrin, sheathless narrow capillary CE/MS with flow rates of low nanoliters/minute (nL/min) was applied to the separation and detection of cathinones and their positional and optical isomers for the first time.Low-flow sheathless CE/MS using a 20-µm-i.d. capillary in conjunction with a porous tip interface was used for the separation of cathinone derivatives and their optical isomers. Highly sulfated γ-cyclodextrin (HS-γ-CD) in conjunction with (+)-18-crown-6-tetracarboxylic acid ((+)-18-C-6-TCA) was used as the BGE and an ion trap mass spectrometer operating in full scan mode was utilized.Utilizing low flow rate (~10 nL/min) sheathless CE/MS, the use of the sodium salt of HS-γ-CD as the BGE was compared with the same solution using PFT. The relative and absolute sensitivity of detection of cathinones were about the same, indicating that under low-flow sheathless CE/MS there was no significant suppression due to the existence of HS-γ-CD in the electrospray process. However, enhanced resolution of cathinone derivatives and their positional and optical isomers was observed when the solution of HS-γ-CD was used as the BGE. The enhanced resolution was because of the presence of the HS-γ-CD in the entire capillary during the analysis. The addition of 15 mM (+)-18-C-6-TCA to the BGE containing HS-γ-CD further enhanced the resolution resulting in separation of all cathinones and their positional and optical isomers.A novel CE/MS technique has been introduced that combines low-flow sheathless CE/MS, with HS-γ-CD and 15 mM (+)-18-C-6-TCA as the BGE for separation of cathinone derivatives as well as their positional and optical isomers.
Gas chromatography/chemical reaction interface mass spectrometry (GC/CRIMS) is shown to be a successful selective method for the detection of selenium-containing compounds. Two reaction gases, sulfur dioxide (SO2) and hydrogen chloride (HCl), were examined in order to optimize selectivity and sensitivity. A high degree of selectivity was obtained with SO2 as a reaction gas; however, the detection limit of 80SeO3+ at m/z 128 (the most sensitive ion for the SO2-containing plasma) was only 3 ng μl-1. HCl gas, which had been shown to be a good reaction gas for sulfur-containing compounds, was also shown to be an excellent reaction gas for selenium-containing compounds. In the HCl-containing plasma, 80SeCl+ at m/z 115 was the most sensitive and selective ion for the detection of selenium-containing compounds. Selectivity was demonstrated by using mixtures of selenium-containing and non-selenium-containing compounds. The utility of GC/CRIMS as a method for the selective detection of selenium-containing compounds was demonstrated with a variety of selenium complexes that were formed by the addition of selective selenium complexing agents to selenium-containing water. The detection limit of selenium in water was ∽62 pg and the linear dynamic range spanned at least two orders of magnitude (620 pg μl-1–308 ng μl-1).
Capillary electrophoresis/electrospray ionization (CE/ESI) high mass accuracy time-of-flight mass spectrometry was used for the first time to characterize small proteins using peptide mapping. To identify small proteins, the intact proteins were first analyzed to obtain their average molecular weights with errors less than 1 Da. On-line capillary electrophoresis mass spectrometry of the tryptic digests of these small proteins was then performed to obtain the accurate molecular weights of the peptides with accuracies of approximately 10 ppm. Next, this information was used for the identification of the proteins using a protein database. It was found that high mass accuracy is an effective tool in reducing the list of most-likely proteins generated by the database. In addition, on-line collision-induced dissociation of the completely or partially resolved capillary electrophoresis peaks of the protein digests was used to unambiguously identify the sequences of these peptides. Each CE/ESI-MS analysis used only 5 nL of sample containing approximately 120 fmol of each peptide in protein digests. The results indicate that the combination of capillary electrophoresis and high resolution, high mass accuracy time-of-flight mass spectrometry is a viable option for the identification of small proteins using peptide mapping.
An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
Synchrotron radiation (SR) has become a preferred technique for the analysis of a wide range of archeological samples, artwork, and museum specimens. While SR is called a nondestructive technique, its effect on proteinaceous specimens has not been fully investigated at the molecular level. To investigate the molecular level effects of synchrotron X-ray on proteinaceous specimens, we propose a methodology where four variables are considered: (1) type of specimen: samples ranging from amino acids to proteinaceous objects such as silk, wool, parchment, and rabbit skin glue were irradiated; (2) synchrotron X-ray energy; (3) beam intensity; (4) irradiation time. Irradiated specimens were examined for both macroscopic and molecular effects. At macroscopic levels, color change, brittleness, and solubility enhancement were observed for several samples within 100 s of irradiation. At molecular levels, the method allowed one to quantify significant amino acid modifications. Aspartic acid (Asp), wool, parchment, and rabbit skin glue showed a significant increase in Asp racemization upon increasing irradiation time with rabbit skin glue showing the greatest increase in d-Asp formation. In contrast, Asp in silk, pure cystine (dimer of cysteine), and asparagine (Asn) did not show signs of racemization at the irradiation times studied; however, the latter two compounds showed significant signs of decomposition. Parchment and rabbit skin glue exhibited racemization of Asp, as well as racemization of isoleucine (Ile) and phenylalanine (Phe) after 100 s of irradiation with a focused beam. Under the experimental conditions and sample type and dimensions used here, more change was observed for focused and low energy (8 keV) beams than unfocused or higher energy (22 keV) beams. These results allow quantification of the change induced at the molecular level on proteinaceous specimens by synchrotron X-ray radiation and help to define accurate thresholds to minimize the probability of damage occurring to cultural heritage specimens. For most samples, damage was usually observed in the 1-10 s time scale, which is about an order of magnitude longer than SR studies of cultural heritage under X-ray fluorescence (XRF) mode; however, it is consistent with the duration of X-ray absorption spectroscopy (XAS) and microcomputed tomography (μCT) measurements.
