Performance for proton anisotropic flow measurement of the CBM experiment at FAIR

The Compressed Baryonic Matter experiment (CBM) performance for proton anisotropic flow measurements is studied with Monte-Carlo simulations using collisions of gold ions at lab momentum of 12A GeV/c employing DCM-QGSM-SMM heavy-ion event generator. Realistic procedures are used for centrality estimation with the number of registered tracks and particle identification with information from Time-Of-Flight detector. Variation of directed flow estimates depending on various combinations of PSD modules is used to evaluate possible systematic biases due to collision symmetry plane estimation

Using multiplicity of produced particles for centrality determination in heavy-ion collisions with the CBM experiment

The evolution of matter created in a heavy-ion collision depends on its initial geometry. Experimentally collision geometry is characterized with centrality. Procedure of centrality determination for the Compressed Baryonic Matter (CBM) experiment at FAIR is presented. Relation between parameters of the collision geometry (such as impact parameter magnitude) and centrality classes is extracted using multiplicity of produced charged particles. The latter is connected to the collision geometry parameters using Monte-Carlo Glauber approach

The very forward hadron calorimeter PSD for the future CBM@FAIR experiment

The Projectile Spectator Detector (PSD) of the CBM experiment at the future FAIR facility is a compensating lead-scintillator calorimeter designed to measure the energy distribution of the forward going projectile nucleons and nuclei fragments (reaction spectators) produced close to the beam rapidity. The detector performance for the centrality and reaction plane determination is re- viewed based on Monte-Carlo simulations of gold-gold collisions by means of four different heavy-ion event generators. The PSD energy resolution and the linearity of the response measured at CERN PS for the PSD supermodule consisting of 9 modules are presented. Predictions of the calorimeter radiation conditions at CBM and response measurement of one PSD module equipped with neutron irradiated MPPCs used for the light read out are discussed

Challenges in QCD matter physics - The Compressed Baryonic Matter experiment at FAIR

Substantial experimental and theoretical efforts worldwide are devoted to explore the phase diagram of strongly interacting matter. At LHC and top RHIC energies, QCD matter is studied at very high temperatures and nearly vanishing net-baryon densities. There is evidence that a Quark-Gluon-Plasma (QGP) was created at experiments at RHIC and LHC. The transition from the QGP back to the hadron gas is found to be a smooth cross over. For larger net-baryon densities and lower temperatures, it is expected that the QCD phase diagram exhibits a rich structure, such as a first-order phase transition between hadronic and partonic matter which terminates in a critical point, or exotic phases like quarkyonic matter. The discovery of these landmarks would be a breakthrough in our understanding of the strong interaction and is therefore in the focus of various high-energy heavy-ion research programs. The Compressed Baryonic Matter (CBM) experiment at FAIR will play a unique role in the exploration of the QCD phase diagram in the region of high net-baryon densities, because it is designed to run at unprecedented interaction rates. High-rate operation is the key prerequisite for high-precision measurements of multi-differential observables and of rare diagnostic probes which are sensitive to the dense phase of the nuclear fireball. The goal of the CBM experiment at SIS100 (sqrt(s_NN) = 2.7 - 4.9 GeV) is to discover fundamental properties of QCD matter: the phase structure at large baryon-chemical potentials (mu_B > 500 MeV), effects of chiral symmetry, and the equation-of-state at high density as it is expected to occur in the core of neutron stars. In this article, we review the motivation for and the physics programme of CBM, including activities before the start of data taking in 2022, in the context of the worldwide efforts to explore high-density QCD matter.Comment: 15 pages, 11 figures. Published in European Physical Journal

Binding of Different Cyclosporin Variants to Micelles Evidenced by NMR and MD Simulations

Peptides play a critical role in the life of organisms, performing completely different functions. The biological activity of some peptides, such as cyclosporins, can be determined by the degree of membrane permeability. Thus, it becomes important to study how the molecule interacts with lipid bilayers. Cyclosporins C, E, H and L were characterised molecular dynamics simulation; NMR spectroscopy studies were also carried out for cyclosporins C and E. The comparison of one- and two-dimensional spectra revealed certain similarities between spatial structures of the studied cyclosporin variants. Upon dissolving in water containing DPC micelles, which serve as model membranes, subtle changes in the NMR spectra appear, but in a different way for different cyclosporins. In order to understand whether observed changes are related to any structural modifications, simulation of the interaction of the peptide with the phospholipid micelle was performed. The onset of the interaction was observed, when the peptide is trapped to the surface of the micelle. Simulations of this kind are also of interest in the light of the well-known membrane permeability of cyclosporin, which is important for its biological action

Binding of Different Cyclosporin Variants to Micelles Evidenced by NMR and MD Simulations

Peptides play a critical role in the life of organisms, performing completely different functions. The biological activity of some peptides, such as cyclosporins, can be determined by the degree of membrane permeability. Thus, it becomes important to study how the molecule interacts with lipid bilayers. Cyclosporins C, E, H and L were characterised molecular dynamics simulation; NMR spectroscopy studies were also carried out for cyclosporins C and E. The comparison of one- and two-dimensional spectra revealed certain similarities between spatial structures of the studied cyclosporin variants. Upon dissolving in water containing DPC micelles, which serve as model membranes, subtle changes in the NMR spectra appear, but in a different way for different cyclosporins. In order to understand whether observed changes are related to any structural modifications, simulation of the interaction of the peptide with the phospholipid micelle was performed. The onset of the interaction was observed, when the peptide is trapped to the surface of the micelle. Simulations of this kind are also of interest in the light of the well-known membrane permeability of cyclosporin, which is important for its biological action

Nanoparticles of Cerium Dioxide and Pristine (Unmodified) Fullerene C60 Protect Living Cells against Adverse Environmental Exposure: Does it Work?

We believe that unmodified hydrated C60 fullerene (C60FWS) and nanocrystalline cerium dioxide (NCD) are promising for biological research. It is knowns that these nanoparticles protect living cells from damaging environmental factors such as radioactive and ultraviolet radiation, temperature, hypoxia, toxic substances, etc. However, little attention has been paid in scientific reports to the use and study of these nanoparticles as possible adaptogens. In our studies, we tried to protect the culture of cyanobacteria Spirulina platensis with C60 and NCD from adverse conditions. The choice of Spirulina platensis is due to its sensitivity to adverse environmental factors. The results obtained show that the absence of toxic effects of C60 and NCD of selected concentrations on the Spirulina platensis culture has been found. Nanoparticles C60 and NCD maintained the culture of Spirulina platensis for at least 4 weeks in the absence of nutrients, light, low pH storage conditions and low temperature. Cyanobacteria stored for 1–4 weeks in distilled water with nanoparticles showed increased proliferative activity compared to samples stored at the same time in the standard Zarrouk’s nutrient medium. Keywords: fullerene C60, nanocrystalline cerium dioxide, Spirulina platensis, adaptogens

Use of a combination of the RDC method and NOESY NMR spectroscopy to determine the structure of Alzheimer’s amyloid Aβ10–35 peptide in solution and in SDS micelles

The spatial structure of Alzheimer's amyloid A beta(10-35)-NH2 peptide in aqueous solution at pH 7.3 and in SDS micelles was investigated by use of a combination of the residual dipolar coupling method and two-dimensional NMR spectroscopy (TOCSY, NOESY). At pH 7.3 A beta(10-35)-NH2 adopts a compact random-coil conformation whereas in SDS micellar solutions two helical regions (residues 13-23 and 30-35) of A beta(10-35)-NH2 were observed. By use of experimental data, the structure of "peptide-micelle" complex was determined; it was found that A beta(10-35)-NH2 peptide binds to the micelle surface at two regions (residues 17-20 and 29-35)

Spatial structure of oligopeptide PAP(248-261), the N-terminal fragment of the HIV enhancer prostatic acid phosphatase peptide PAP(248-286), in aqueous and SDS micelle solutions

Prostatic acid phosphatase (PAP) is an enzyme that facilitates infection of cells by HIV. Its peptide fragment PAP(248-286) forms amyloid fibrils known as SEVI, which enhance attachment of the virus by viral adhesion to the host cell prior to receptor-specific binding via reducing the electrostatic repulsion between the membranes of the virus and the target cell. The secondary structure of PAP(248-286) in aqueous and SDS solutions can be divided into an N-terminal disordered region, an α-helical central part and an α/310-helical C-terminal region (Nanga et al., 2009). In this work, we used NMR spectroscopy to study the spatial structure of the isolated N-terminal fragment of PAP(248-286), PAP(248-261) (GIHKQKEKSRLQGG), in aqueous and SDS micelle solutions. Formation of a PAP(248-261)-SDS complex was confirmed by chemical shift alterations in the 1H NMR spectra of the peptide, as well as by the signs and values of Nuclear Overhauser Effect (NOE). In addition, the PAP(248-261) peptide does not form any specified secondary structure in either aqueous or SDS solutions

Mitochondrial potential (ΔΨ

Rare-earth-based nanoparticles (NPs) are widely used as fluorescent probes for imaging in vitro and in vivo. One of the challenges that restrain NPs applications in biomedical research is their effect on subcellular structures. In this paper, the ability of lanthanide NPs to affect the cellular oxidative balance and alter the mitochondrial function was analyzed. Since size and shape mutually affect the cellular internalization and intracellular distribution of NPs, the investigations were performed with NPs of spherical (GdYVO4:Eu3+, spindle-(GdVO4: Eu3+ and rod-like (LaVO4: Eu3+ shapes. Quantitative microfluorimetry with JC-1 (5,5′,6,6′-tetrachloro-1,1′,3,3′-tetraethylbenzimidazolocarbocyanine iodide) as a mitochondrial probe was used for monitoring of the mitochondrial transmembrane potential (ΔΨ m) in single living cells. Changes in the ratio of the JC-1 probe fluorescence were used to analyze the NPs effect on ΔΨ m. The fastest suppressive effect (within 1 hour) was found for spherical NPs. Gradual lowering of ΔΨ m was observed at the exposure of cells within 24 hours for all types of NPs. Exogenous thiols were required for ΔΨ m protection. The protective role of exogenous glutathione (GSH) proves that the increase of reactive oxygen species (ROS) formation with depletion of GSH can mediate NPs toxicity. The dynamics of the shape-dependent effect can be explained by the features of NPs transportation into cells