| 1. |
- Hellmann, S., et al.
(författare)
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Time-resolved x-ray photoelectron spectroscopy at FLASH
- 2012
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Ingår i: New Journal of Physics. - : IOP Publishing. - 1367-2630. ; 14
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Tidskriftsartikel (refereegranskat)abstract
- The technique of time-resolved pump-probe x-ray photoelectron spectroscopy using the free-electron laser in Hamburg (FLASH) is described in detail. Particular foci lie on the macrobunch resolving detection scheme, the role of vacuum space-charge effects and the synchronization of pump and probe lasers. In an exemplary case study, the complete Ta 4f core-level dynamics in the layered charge-density-wave (CDW) compound 1T-TaS2 in response to impulsive optical excitation is measured on the sub-picosecond to nanosecond timescale. The observed multi-component dynamics is related to the intrinsic melting and reformation of the CDW as well as to extrinsic pump-laser-induced vacuum space-charge effects.
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| 2. |
- Hellmann, S., et al.
(författare)
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Ultrafast Melting of a Charge-Density Wave in the Mott Insulator 1T-TaS2
- 2010
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Ingår i: Physical Review Letters. - 1079-7114. ; 105:18
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Tidskriftsartikel (refereegranskat)abstract
- Femtosecond time-resolved core-level photoemission spectroscopy with a free-electron laser is used to measure the atomic-site specific charge-order dynamics of the charge-density wave in the Mott insulator 1T-TaS2. After strong photoexcitation, a prompt loss of charge order and subsequent fast equilibration dynamics of the electron-lattice system are observed. On the time scale of electron-phonon thermalization, about 1 ps, the system is driven across a phase transition from a long-range charge ordered state to a quasiequilibrium state with domainlike short-range charge and lattice order. The experiment opens the way to study the nonequilibrium dynamics of condensed matter systems with full elemental, chemical, and atomic-site selectivity.
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| 3. |
- Marczynski, M., et al.
(författare)
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Charged glycan residues critically contribute to the adsorption and lubricity of mucins
- 2019
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Ingår i: Colloids and Surfaces B. - : Elsevier B.V.. - 0927-7765 .- 1873-4367.
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Tidskriftsartikel (refereegranskat)abstract
- In the human body, mucin glycoproteins efficiently reduce friction between tissues and thereby protect the mucosa from mechanical damage. Mucin lubricity is closely related to their molecular structure: it has been demonstrated previously that the hydrophobic termini of mucins critically contribute to their lubricity. If and how intrinsic sources of negative charge in mucins, e.g., sulfated glycans and sialic acid residues, are relevant for the tribological behavior of mucin solutions has, however, not been addressed yet. In this manuscript, we show that the removal of either sialic acid or sulfate groups, which comprise only a minor amount of the total molecular weight, from MUC5B drastically reduces its lubricity. For MUC5AC solutions, however, this effect only occurs once mucin-associated DNA is removed as well. We find that neither the hydration state nor the average conformation of mucins adsorbed onto hydrophilic or hydrophobic surfaces is affected by the removal of anionic sugars. Instead, our data suggests that a loss of anionic sugars mainly influences the dynamic adsorption process of mucins onto both hydrophilic and hydrophobic surfaces.
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| 4. |
- Jiang, Kun, et al.
(författare)
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Modulating the Bioactivity of Mucin Hydrogels with Crosslinking Architecture
- 2021
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Ingår i: Advanced Functional Materials. - : Wiley. - 1616-301X .- 1616-3028. ; 31:10
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Tidskriftsartikel (refereegranskat)abstract
- Hydrogels made of crosslinked macromolecules used in regenerative medicine technologies can be designed to affect the fate of surrounding cells and tissues in defined ways. Their function typically depends on the type and number of bioactive moieties such as receptor ligands present in the hydrogel. However, the detail in how such moieties are presented to cells can also be instrumental. In this work, how the crosslinking architecture of a hydrogel can affect its bioactivity is explored. It is shown that bovine submaxillary mucins, a highly glycosylated and immune-modulating protein, exhibit strikingly different bioactivities whether they are crosslinked through their glycans or their protein domains. Both the susceptibility to enzymatic degradation and macrophage response are affected, while rheological properties and barrier to diffusion are mostly unaffected. The results suggest that crosslinking architecture affects the accessibility of the substrate to proteases and the pattern of sialic acid residues exposed to the macrophages. Thus, modulating the accessibility of binding sites through the choice of the crosslinking strategy appears as a useful parameter to tune the bioactivity of hydrogel-based systems.
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