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| 2. |
- Gopakumar, Geethanjali, 1992-, et al.
(författare)
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X-ray Induced Fragmentation of Protonated Cystine
- 2022
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Ingår i: Journal of Physical Chemistry A. - : American Chemical Society (ACS). - 1089-5639 .- 1520-5215. ; 126:9, s. 1496-1503
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Tidskriftsartikel (refereegranskat)abstract
- We demonstrate site-specific X-ray induced fragmentation across the sulfur L-edge of protonated cystine, the dimer of the amino acid cysteine. Ion yield NEXAFS were performed in the gas phase using electrospray ionization (ESI) in combination with an ion trap. The interpretation of the sulfur L-edge NEXAFS spectrum is supported by Restricted Open-Shell Configuration Interaction (ROCIS) calculations. The fragmentation pathway of triply charged cystine ions was modeled by Molecular Dynamics (MD) simulations. We have deduced a possible pathway of fragmentation upon excitation and ionization of S 2p electrons. The disulfide bridge breaks for resonant excitation at lower photon energies but remains intact upon higher energy resonant excitation and upon ionization of S 2p. The larger fragments initially formed subsequently break into smaller fragments.
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| 3. |
- Leroux, Juliette, et al.
(författare)
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Mapping the electronic transitions of protonation sites in peptides using soft X-ray action spectroscopy
- 2023
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Ingår i: Physical Chemistry, Chemical Physics - PCCP. - : Royal Society of Chemistry. - 1463-9076 .- 1463-9084. ; 25:37, s. 25603-25618
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Tidskriftsartikel (refereegranskat)abstract
- Near-edge X-ray absorption mass spectrometry (NEXAMS) around the nitrogen and oxygen K-edges was employed on gas-phase peptides to probe the electronic transitions related to their protonation sites, namely at basic side chains, the N-terminus and the amide oxygen. The experimental results are supported by replica exchange molecular dynamics and density-functional theory and restricted open-shell configuration with single calculations to attribute the transitions responsible for the experimentally observed resonances. We studied five tailor-made glycine-based pentapeptides, where we identified the signature of the protonation site of N-terminal proline, histidine, lysine and arginine, at 406 eV, corresponding to N 1s & RARR; & sigma;*(NHx+) (x = 2 or 3) transitions, depending on the peptides. We compared the spectra of pentaglycine and triglycine to evaluate the sensitivity of NEXAMS to protomers. Separate resonances have been identified to distinguish two protomers in triglycine, the protonation site at the N-terminus at 406 eV and the protonation site at the amide oxygen characterized by a transition at 403.1 eV.
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| 4. |
- Marçal, Lucas A.B., et al.
(författare)
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In Situ Imaging of Ferroelastic Domain Dynamics in CsPbBr3Perovskite Nanowires by Nanofocused Scanning X-ray Diffraction
- 2020
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Ingår i: ACS Nano. - : American Chemical Society (ACS). - 1936-0851 .- 1936-086X. ; 14:11, s. 15973-15982
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Tidskriftsartikel (refereegranskat)abstract
- The interest in metal halide perovskites has grown as impressive results have been shown in solar cells, light emitting devices, and scintillators, but this class of materials have a complex crystal structure that is only partially understood. In particular, the dynamics of the nanoscale ferroelastic domains in metal halide perovskites remains difficult to study. An ideal in situ imaging method for ferroelastic domains requires a challenging combination of high spatial resolution and long penetration depth. Here, we demonstrate in situ temperature-dependent imaging of ferroelastic domains in a single nanowire of metal halide perovskite, CsPbBr3. Scanning X-ray diffraction with a 60 nm beam was used to retrieve local structural properties for temperatures up to 140 °C. We observed a single Bragg peak at room temperature, but at 80 °C, four new Bragg peaks appeared, originating in different real-space domains. The domains were arranged in periodic stripes in the center and with a hatched pattern close to the edges. Reciprocal space mapping at 80 °C was used to quantify the local strain and lattice tilts, revealing the ferroelastic nature of the domains. The domains display a partial stability to further temperature changes. Our results show the dynamics of nanoscale ferroelastic domain formation within a single-crystal perovskite nanostructure, which is important both for the fundamental understanding of these materials and for the development of perovskite-based devices.
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| 5. |
- Marçal, Lucas A.B., et al.
(författare)
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Inducing ferroelastic domains in single-crystal CsPbBr3 perovskite nanowires using atomic force microscopy
- 2021
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Ingår i: Physical Review Materials. - 2475-9953. ; 5:6
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Tidskriftsartikel (refereegranskat)abstract
- Ferroelectric and ferroelastic domains have been predicted to enhance metal halide perovskite (MHP) solar cell performance. While the formation of such domains can be modified by temperature, pressure, or strain, established methods lack spatial control at the level of single domains. Here, we induce the formation of ferroelastic domains in CsPbBr3 nanowires at room temperature using an atomic force microscope (AFM) tip and visualize the domains using nanofocused x-ray diffraction with a 60 nm beam. Regions scanned with a low AFM tip force show orthorhombic 004 reflections along the nanowire axis, while regions exposed to higher forces exhibit 220 reflections. The applied stress locally changes the crystal structure, leading to lattice tilts that define ferroelastic domains, which spread spatially and terminate at {112}-type domain walls. The ability to induce individual ferroelastic domains within MHPs using AFM gives new possibilities for device design and fundamental experimental studies.
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| 6. |
- Markou, Andrea, et al.
(författare)
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Molecular mechanisms governing aquaporin relocalisation
- 2022
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Ingår i: Biochimica et Biophysica Acta - Biomembranes. - : Elsevier BV. - 0005-2736. ; 1864:4
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Tidskriftsartikel (refereegranskat)abstract
- The aquaporins (AQPs) form a family of integral membrane proteins that facilitate the movement of water across biological membrane by osmosis, as well as facilitating the diffusion of small polar solutes. AQPs have been recognised as drug targets for a variety of disorders associated with disrupted water or solute transport, including brain oedema following stroke or trauma, epilepsy, cancer cell migration and tumour angiogenesis, metabolic disorders, and inflammation. Despite this, drug discovery for AQPs has made little progress due to a lack of reproducible high-throughput assays and difficulties with the druggability of AQP proteins. However, recent studies have suggested that targetting the trafficking of AQP proteins to the plasma membrane is a viable alternative drug target to direct inhibition of the water-conducting pore. Here we review the literature on the trafficking of mammalian AQPs with a view to highlighting potential new drug targets for a variety of conditions associated with disrupted water and solute homeostasis.
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| 7. |
- Svensson, Pamela, et al.
(författare)
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Heavy element incorporation in nitroimidazole radiosensitizers : molecular-level insights into fragmentation dynamics
- 2024
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Ingår i: Physical Chemistry, Chemical Physics - PCCP. - : Royal Society of Chemistry. - 1463-9076 .- 1463-9084. ; 26:2, s. 770-779
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Tidskriftsartikel (refereegranskat)abstract
- The present study investigates the photofragmentation behavior of iodine-enhanced nitroimidazole-based radiosensitizer model compounds in their protonated form using near-edge X-ray absorption mass spectrometry and quantum mechanical calculations. These molecules possess dual functionality: improved photoabsorption capabilities and the ability to generate species that are relevant to cancer sensitization upon photofragmentation. Four samples were investigated by scanning the generated fragments in the energy regions around C 1s, N 1s, O 1s, and I 3d-edges with a particular focus on NO2+ production. The experimental summed ion yield spectra are explained using the theoretical near-edge X-ray absorption fine structure spectrum based on density functional theory. Born-Oppenheimer-based molecular dynamics simulations were performed to investigate the fragmentation processes.
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| 8. |
- Unger, Lucas, et al.
(författare)
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Candida albicans induces neutrophil extracellular traps and leucotoxic hypercitrullination via candidalysin
- 2023
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Ingår i: Embo Reports. - : John Wiley & Sons. - 1469-221X .- 1469-3178. ; 24:11
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Tidskriftsartikel (refereegranskat)abstract
- The peptide toxin candidalysin, secreted by Candida albicans hyphae, promotes stimulation of neutrophil extracellular traps (NETs). However, candidalysin alone triggers a distinct mechanism for NET-like structures (NLS), which are more compact and less fibrous than canonical NETs. Candidalysin activates NADPH oxidase and calcium influx, with both processes contributing to morphological changes in neutrophils resulting in NLS formation. NLS are induced by leucotoxic hypercitrullination, which is governed by calcium-induced protein arginine deaminase 4 activation and initiation of intracellular signalling events in a dose- and time-dependent manner. However, activation of signalling by candidalysin does not suffice to trigger downstream events essential for NET formation, as demonstrated by lack of lamin A/C phosphorylation, an event required for activation of cyclin-dependent kinases that are crucial for NET release. Candidalysin-triggered NLS demonstrate anti-Candida activity, which is resistant to nuclease treatment and dependent on the deprivation of Zn2+. This study reveals that C. albicans hyphae releasing candidalysin concurrently trigger canonical NETs and NLS, which together form a fibrous sticky network that entangles C. albicans hyphae and efficiently inhibits their growth.
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