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Hydrogen isotope analysis in W-tiles using fs-LIBS.

ABSTRACT: Laser-Induced Breakdown Spectroscopy (LIBS) is a promising technology for in-situ analysis of Plasma-Facing Components in magnetic confinement fusion facilities. It is of major interest to monitor the hydrogen isotope retention i.e. tritium and deuterium over many operation hours to guarantee safety and availability of the future reactor. In our studies we use ultraviolet femtosecond laser pulses to analyze tungsten (W) tiles that were exposed to a deuterium plasma in the linear plasma device PSI-2, which mimics conditions at the first wall. A high-resolution spectrometer is used to detect the Balmer-[Formula: see text] transition of the surface from implanted hydrogen isotopes (H and D). We use Calibration Free CF-LIBS to quantify the amount of deuterium stored in W. This proof-of-principle study shows the applicability of femtosecond lasers for the detection of low deuterium concentration as present in first wall material of prevailing fusion experiments.

SUBMITTER: Mittelmann S

PROVIDER: S-EPMC9911398 | biostudies-literature | 2023 Feb

REPOSITORIES: biostudies-literature

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Hydrogen isotope analysis in W-tiles using fs-LIBS.

Mittelmann Steffen S Touchet Kévin K Mao Xianglei X Park Minok M Brezinsek Sebastijan S Pretzler Georg G Zorba Vassilia V

Scientific reports 20230209 1

Laser-Induced Breakdown Spectroscopy (LIBS) is a promising technology for in-situ analysis of Plasma-Facing Components in magnetic confinement fusion facilities. It is of major interest to monitor the hydrogen isotope retention i.e. tritium and deuterium over many operation hours to guarantee safety and availability of the future reactor. In our studies we use ultraviolet femtosecond laser pulses to analyze tungsten (W) tiles that were exposed to a deuterium plasma in the linear plasma device PS ...[more]

PMID: 36759588

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Project description:Self-assembled cyclic peptide nanotubes with alternating D- and L-amino acid residues in the sequence of each subunit have attracted a great deal of attention due to their potential for new nanotechnology and biomedical applications, mainly in the field of antimicrobial peptides. Molecular dynamics simulations can be used to characterize these systems with atomic resolution at different time scales, providing information that is difficult to obtain via wet lab experiments. However, the performance of classical force fields typically employed in the simulation of biomolecules has not yet been extensively tested with this kind of highly constrained peptide. Four different classical force fields (AMBER, CHARMM, OPLS, and GROMOS), using a nanotube formed by eight D,L-α-cyclic peptides inserted into a lipid bilayer as a model system, were employed here to fill this gap. Significant differences in the pseudo-cylindrical cavities formed by the nanotubes were observed, the most important being the diameter of the nanopores, the number and location of confined water molecules, and the density distribution of the solvent molecules. Furthermore, several modifications were performed on GROMOS54a7, aiming to explore acceleration strategies of the MD simulations. The hydrogen mass repartitioning (HMR) and hydrogen isotope exchange (HIE) methods were tested to slow down the fastest degrees of freedom. These approaches allowed a significant increase in the time step employed in the equation of the motion integration algorithm, from 2 fs up to 5-7 fs, with no serious changes in the structural and dynamical properties of the nanopores. Subtle differences with respect to the simulations with the unmodified force fields were observed in the concerted movements of the cyclic peptides, as well as in the lifetime of several H-bonds. All together, these results are expected to contribute to better understanding of the behavior of self-assembled cyclic peptide nanotubes, as well as to support the methods tested to speed up general MD simulations; additionally, they do provide a number of quantitative descriptors that are expected to be used as a reference to design new experiments intended to validate and complement computational studies of antimicrobial cyclic peptides.

Dataset Information

Hydrogen isotope analysis in W-tiles using fs-LIBS.

Publications

Hydrogen isotope analysis in W-tiles using fs-LIBS.

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