Development of Water Gridded Ion Thruster for Small Satellites: Toward On-Orbit Demonstration

Water as a propellant has many advantages and does not require a pressure vessel for storage. Its high safety level can reduce development cost and time. It is also a resource tightly tied to human spaceflight and found in-situ in the upcoming moon missions. Stored in its liquid state in our thrusters, it is then vaporized at room temperature and low pressure. The resulted steam is then injected in the discharge chambers where it is transformed into plasma. Plasma generation is achieved through flight-proven microwave discharge using Electron Cyclotron Resonance

Influence of the Metals and Ligands in Dinuclear Complexes on Phosphopeptide Sequencing by Electron Transfer Dissociation Tandem Mass Spectrometry

International audiencePhosphorylation is one of the most important protein modifications, and electron-transfer dissociation tandem mass spectrometry (ETD-MS/MS) is a potentially useful method for the sequencing of phosphopeptides, including determination of the phosphorylation site. Notably, ETD-MS/MS typically provides useful information when the precursor contains more than three positive charges. It is not yet used as an analysis method for large-scale phosphopeptide production due to difficulties occurring in the production of acidic phosphopeptides having more than three positive charges. To increase the charge state of phosphopeptides, we used dinuclear metal complexes, which selectively bind to the phosphate group in phosphopeptides with the addition of positive charge(s). Dinuclear copper, zinc, and gallium complexes were tested and it was found that the type of metal present in the complex strongly affected the affinity of the phosphorylated compounds and their ETD fragmentation. The dinuclear copper complex interacted weakly with the phosphate groups and ETD-induced peptide fragmentation was largely suppressed by the presence of Cu2+, which worked as an electron trap. The dinuclear gallium complex was strongly bound to a phosphate group. However, the ligand binding to gallium acted as an electron trap and the presence of dinuclear gallium complex in the precursor for ETD-MS/MS hampered the sequencing of the phosphopeptides, as in the case of dinuclear copper complexes. In contrast, dinuclear zinc complexes efficiently bind to phosphopeptides with an increase in the charge state, facilitating phosphopeptide sequencing by ETD-MS/MS. The fragmentation of the ligand and peptide backbone in the dinuclear zinc–phosphopeptide complex were competitively induced by ETD. These processes are influenced by the ligand structure and so the detailed ETD fragmentation pathways were investigated using density functional theory calculations

Fragmentation study of tryptophan-derived metabolites induced by electrospray ionization mass spectrometry for highly sensitive analysis

Liquid chromatography–tandem mass spectrometry (LC–MS/MS) is interfaced with electrospray ionization (ESI), which generally produces intact gas-phase ions of biomolecules. However, ESI induces the fragmentation of tryptophan-derived metabolites, which are known to act as neurotransmitters and psychoactive drugs. Tryptophan-derived metabolites undergo N–C α bond dissociation during ESI, producing a fragment ion with a spiro[cyclopropane-indolium] backbone. Fragmentation is suppressed by the presence of an α-carboxyl group and the modification of amino groups. In particular, tryptamine and serotonin, which lack such functional groups, produce more intense fragment-ion signals than protonated molecules. The multiple reaction monitoring (MRM)-based quantitative analysis of tryptamine and serotonin used the fragment ions produced from in-source collision-induced dissociation as the precursor ions, which improved the signal-to-noise ratio of the resulting spectra. The present method allows for the quantitative analysis of tryptamine and serotonin with high sensitivity

Ultraviolet Laser Induced Hydrogen Transfer Reaction: Study of the First Step of MALDI In-Source Decay Mass Spectrometry

The early mechanisms of matrix-assisted laser desorption/ionization in-source decay (MALDI-ISD) are described herein. MALDI-ISD is initiated by the hydrogen transfer from excited matrix molecules to the carbonyl oxygen of the peptide backbone, which is followed by a radical-induced cleavage, producing the c′/z• fragment pair. As expected, the use of 2,5-DHB or 1,5-DAN was efficient to induce MALDI-ISD, and the strongest intensity of MALDI-ISD fragments was observed when laser shots were performed on matrix crystals. In contrast, the hydrogen radical transfer reaction was suppressed by using ionic liquid and amorphous structure of 2,5-DHB and 1,5-DAN mixture as a matrix. Our results suggest that the hydrogen transfer occurs on the matrix crystal during the dissipation of the laser energy and before desorption, following ISD fragments formed in the MALDI plume

In-Source Decay during Matrix-Assisted Laser Desorption/Ionization Combined with the Collisional Process in an FTICR Mass Spectrometer

The type of ions detected after in-source decay (ISD) in a MALDI source differs according to the ion source pressure and on the mass analyzer used. We present the mechanism leading to the final ISD ions for a Fourier transform-ion cyclotron resonance mass spectrometer (FTICR MS). The MALDI ion source was operated at intermediate pressure to cool the resulting ions and increase their lifetime during the long residence times in the FTICR ion optics. This condition produces not only c′, z′, and w fragments, but also a, y′, and d fragments. In particular, d ions help to identify isobaric amino acid residues present near the Nterminal amino acid. Desorbed ions collide with background gas during desorption, leading to proton mobilization from Arg residues to a less favored protonation site. As a result, in the case of ISD with MALDI FTICR, the influence of the Arg residue in ISD fragmentation is less straightforward than for TOF MS and the sequence coverage is thus improved. MALDI-ISD combined with FTICR MS appears to be a useful method for sequencing of peptides and proteins including discrimination of isobaric amino acid residues and site determination of phosphorylation. Additionally we also used new software for in silico elimination of MALDI matrix peaks from MALDI-ISD FTICR mass spectra. The combination of high resolving power of an FTICR analyzer and matrix subtraction software helps to interpret the low m/z region of MALDI-ISD spectra. Finally, several of these developed methods are applied in unison toward a MALDI ISD FTICR imaging experiment on mouse brain to achieve better results

Fatigue Damage Evaluation by Diffraction Contrast Tomography Using Ultra-Bright Synchrotron Radiation

A three-dimensional grain mapping technique for polycrystalline materials, called X-ray diffraction contrast tomography (DCT), was developed at SPring-8, which is the brightest synchrotron radiation facility in Japan. The developed technique was applied to an austenitic stainless steel. The shape and location of grains could be determined by DCT using the apparatus in a beam line of SPring-8. To evaluate the dislocation structure in fatigue, the total misorientation of individual grains was measured by DCT. The average value of the total misorientation over one sample was increased with the number of cycles. In a grain, the change of the total misorientation was largest for the primary slip plane. The maximum change of the total misorientation in fatigue was larger for planes with larger Schmid factor, and the first fatigue crack initiation was occurred in a grain, which had the greatest change of the total misorientation