Artifact quantification of venous stents in the MRI environment: Differences between braided and laser-cut designs

PurposeTo quantify B₀- and B₁-induced imaging artifacts of braided venous stents and to compare the artifacts to a set of laser-cut stents used in venous interventions.MethodsThree prototypes of braided venous stents with different geometries were tested in vitro. B₀ field distortion maps were measured via the frequency shift $\mathrm{\Delta }f$ using multi-echo imaging. B₁ distortions were quantified using the double angle method. The relative amplitudes $B_1^{\mathit{rel}}$ were calculated to compare the intraluminal alteration of B₁. Measurements were repeated with the stents in three different orientations: parallel, diagonal and orthogonal to B₀.ResultsAt 1.5 T, the braided stents induced a maximum frequency shift of $\left|\mathrm{\Delta }f\left(\mathit{x}\right)\right|<100\mathrm{H}\mathrm{z}$. Signal voids were limited to a distance of 2 mm to the stent walls at an echo time of 3 ms. No substantial difference in the B₀ field distortions was seen between laser-cut and braided venous stents. $B_1^{\mathit{rel}}$ maps showed strongly varying distortion patterns in the braided stents with the mean intraluminal $B_1^{\mathit{rel}}$ ranging from $\left(63\pm 18\right)\%$ in prototype 1 to $\left(98\pm 38\right)\%$ in prototype 2. Compared to laser-cut stents the braided stents showed a 5 to 9 times higher coefficient of variation of the intraluminal $B_1^{\mathit{rel}}$.ConclusionBraided venous stent prototypes allow for MR imaging of the intraluminal area without substantial signal voids due to B₀-induced artifacts. Whereas B₁ is attenuated homogeneously in laser-cut stents, the B₁ distortion in braided stents is more inhomogeneous and shows areas with enhanced amplitude. This could potentially be used in braided stent designs for intraluminal signal amplification.     

Penicillium rubens germination on desiccated and nutrient-depleted conditions depends on the water activity during sporogenesis

Fungal growth often appears in a surrounding where water and nutrients are scarce. The impact of this environment during sporogenesis on subsequent growth is often neglected.This study investigates the effect of water availability during sporogenesis on subsequent early growth. Therefore, a carbon-depleted substrate was constructed. Humidity is then the only parameter of interest. The water conditions during sporogenesis, and during subsequent growth, were varied. This is a stressing environment: no carbon source is present, and water provided solely via the vapour.The lag time, $t_l$, and initial growth rate, ${\mu }_{fp}$, of the germ tubes were monitored.The effect of $a_w$ history on germination and initial growth depends on the $RH$ of the environment. Only at low $RH$ do spores produced at low $a_w$ have a smaller $t_l$ and higher ${\mu }_{fp}$ compared to those grown at high $a_w$. This result was remarkably pronounced when the substrate was also made hydrophobic: growth only occurred when spores were developed at low $a_w$ and placed in high $RH$.Spores grown on lowered $a_w$ attract more water. It is hypothesized that this attraction affects subsequent growth behaviour, and is the reason why growth on hydrophobic glass only prevails in the condition of high $RH$ and lowered $a_w$ history.We demonstrate the influence of cultivation conditions on germination, which becomes more pronounced in a more desiccated environment.     

A microdosimetric analysis of the interactions of mono-energetic neutrons with human tissue

Nuclear reactions induced during high-energy radiotherapy produce secondary neutrons that, due to their carcinogenic potential, constitute an important risk for the development of iatrogenic cancer. Experimental and epidemiological findings indicate a marked energy dependence of neutron relative biological effectiveness (RBE) for carcinogenesis, but little is reported on its physical basis. While the exact mechanism of radiation carcinogenesis is yet to be fully elucidated, numerical microdosimetry can be used to predict the biological consequences of a given irradiation based on its microscopic pattern of energy depositions. Building on recent studies, this work investigated the physics underlying neutron RBE by using the microdosimetric quantity dose-mean lineal energy $\left({\bar{y}}_D\right)$ as a proxy. A simulation pipeline was constructed to explicitly calculate the ${\bar{y}}_D$ of radiation fields that consisted of (i) the open source Monte Carlo toolkit Geant4, (ii) its radiobiological extension Geant4-DNA, and (iii) a weighted track-sampling algorithm. This approach was used to study mono-energetic neutrons with initial kinetic energies between 1 eV and 10 MeV at multiple depths in a tissue-equivalent phantom. Spherical sampling volumes with diameters between 2 nm and 1 $\mathrm{\mu }$m were considered. To obtain a measure of RBE, the neutron ${\bar{y}}_D$ values were divided by those of 250 keV X-rays that were calculated in the same way. Qualitative agreement was found with published radiation protection factors and simulation data, allowing for the dependencies of neutron RBE on depth and energy to be discussed in the context of the neutron interaction cross sections and secondary particle distributions in human tissue.     

Significant compaction of H4 histone tail upon charge neutralization by acetylation and its mimics,possible effects on chromatin structure

The intrinsically disordered, positively charged H4 histone tail is important for chromatin structure and function. We have explored conformational ensembles of human H4 tail in solution, with varying levels of charge neutralization via acetylation or amino-acid substitutions such as $K\to Q$. We have employed an explicit water model shown recently to be well suited for simulations of intrinsically disordered proteins.Upon progressive neutralization of the H4, its radius of gyration decreases linearly with the tail charge q, the trend is explained using a simple polymer model. While the wild type state ($q=+8$) is essentially a random coil, hyper-acetylated H4 ($q=+3$) is virtually as compact and stable as a globular protein of the same number of amino-acids.Conformational ensembles of acetylated H4 match the corresponding $K\to X$ substitutions only approximately: based on the ensemble similarity, we propose $K\to M$ as a possible alternative to the commonly used $K\to Q$.Possible effects of the H4 tail compaction on chromatin structure are discussed within a qualitative model in which the chromatin is highly heterogeneous, easily inter-converting between various structural forms. We predict that upon progressive charge neutralization of the H4 tail, the least compact sub-states of chromatin de-condense first, followed by de-condensation of more compact structures, e.g. those that harbor a high fraction of stacked di-nucleosomes. The predicted hierarchy of DNA accessibility increase upon progressive acetylation of H4 might be utilized by the cell for selective DNA accessibility control.     

Crowding-induced protein destabilization in the absence of soft attractions

It is generally assumed that volume exclusion by macromolecular crowders universally stabilizes the native states of proteins and destabilization suggests soft attractions between crowders and protein. Here we show that proteins can be destabilized even by crowders that are purely repulsive. With a coarse-grained sequence-based model, we study the folding thermodynamics of two sequences with different native folds, a helical hairpin and a β-barrel, in a range of crowder volume fractions, ${\phi }_{\text{c}}$. We find that the native state, N, remains structurally unchanged under crowded conditions, while the size of the unfolded state, U, decreases monotonically with ${\phi }_{\text{c}}$. Hence, for all ${\phi }_{\text{c}}>0$, U is entropically disfavored relative to N. This entropy-centric view holds for the helical hairpin protein, which is stabilized under all crowded conditions as quantified by changes in either the folding midpoint temperature, $T_{\text{m}}$, or the free energy of folding. We find, however, that the β-barrel protein is destabilized under low-T, low-${\phi }_{\text{c}}$ conditions. This destabilization can be understood from two characteristics of its folding: 1) a relatively compact U at $T<T_{\text{m}}$, such that U is only weakly disfavored entropically by the crowders; and 2) a transient, compact, and relatively low-energy nonnative state that has a maximum population of only a few percent at ${\phi }_{\text{c}}=0$, but increasing monotonically with ${\phi }_{\text{c}}$. Overall, protein destabilization driven by hard-core effects appears possible when a compaction of U leads to even a modest population of compact nonnative states that are energetically competitive with N.