The upper and lower solution method for nonlinear third-order three-point boundary value problem

This paper is concerned with the following nonlinear third-order three-point boundary value problem \left\{ \begin{array}{l} u^{\prime \prime \prime }(t)+f\left( t,u\left( t\right) ,u^{\prime}\left(t\right) \right) =0,\, t\in \left[ 0,1\right], \\ u\left( 0\right) =u^{\prime }\left( 0\right) =0,\, u^{\prime}\left( 1\right) =\alpha u^{\prime }\left( \eta \right),\label{1.1} \end{array} \right. where $0<\eta <1$ and $0\leq \alpha <1.$ A new maximum principle is established and some existence criteria are obtained for the above problem by using the upper and lower solution method

Observing the origin of superconductivity in quantum critical metals

Despite intense efforts during the last 25 years, the physics of unconventional superconductors, including the cuprates with a very high transition temperature, is still a controversial subject. It is believed that superconductivity in many of these strongly correlated metallic systems originates in the physics of quantum phase transitions, but quite diverse perspectives have emerged on the fundamentals of the electron-pairing physics, ranging from Hertz style critical spin fluctuation glue to the holographic superconductivity of string theory. Here we demonstrate that the gross energy scaling differences that are behind these various pairing mechanisms are directly encoded in the frequency and temperature dependence of the dynamical pair susceptibility. This quantity can be measured directly via the second order Josephson effect and it should be possible employing modern experimental techniques to build a `pairing telescope' that gives a direct view on the origin of quantum critical superconductivity.Comment: 19 pages, 9 figures; minor changes in the experimental part; added a new appendix section calculating the pair susceptibility of marginal Fermi liqui

Pharmacokinetic/Pharmacodynamic Correlation of Cefquinome Against Experimental Catheter-Associated Biofilm Infection Due to Staphylococcus aureus.

Biofilm formations play an important role in Staphylococcus aureus pathogenesis and contribute to antibiotic treatment failures in biofilm-associated infections. The aim of this study was to evaluate the pharmacokinetic/pharmacodynamic (PK/PD) profiles of cefquinome against an experimental catheter-related biofilm model due to S. aureus, including three clinical isolates and one non-clinical isolate. The minimal inhibitory concentration (MIC), minimal biofilm inhibitory concentration (MBIC), biofilm bactericidal concentration (BBC), minimal biofilm eradication concentration (MBEC) and biofilm prevention concentration (BPC) and in vitro time-kill curves of cefquinome were studied in both planktonic and biofilm cells of study S. aureus strains. The in vivo post-antibiotic effects (PAEs), PK profiles and efficacy of cefquinome were performed in the catheter-related biofilm infection model in murine. A sigmoid E max model was utilized to determine the PK/PD index that best described the dose-response profiles in the model. The MICs and MBICs of cefquinome for the four S. aureus strains were 0.5 and 16 μg/mL, respectively. The BBCs (32-64 μg/mL) and MBECs (64-256 μg/mL) of these study strains were much higher than their corresponding BPC values (1-2 μg/mL). Cefquinome showed time-dependent killing both on planktonic and biofilm cells, but produced much shorter PAEs in biofilm infections. The best-correlated PK/PD parameters of cefquinome for planktonic and biofilm cells were the duration of time that the free drug level exceeded the MIC (fT &gt; MIC, R (2) = 96.2%) and the MBIC (fT &gt; MBIC, R (2) = 94.7%), respectively. In addition, the AUC24h/MBIC of cefquinome also significantly correlated with the anti-biofilm outcome in this model (R (2) = 93.1%). The values of AUC24h/MBIC for biofilm-static and 1-log10-unit biofilm-cidal activity were 22.8 and 35.6 h; respectively. These results indicate that the PK/PD profiles of cefquinome could be used as valuable guidance for effective dosing regimens treating S. aureus biofilm-related infections

Bis[2-(benzimidazol-2-ylsulfan­yl)acetato]bis­(2,2′-bipyridine)cadmium(II)

In the structure of the title compound, [Cd(C9H7N2O2S)2(C10H8N2)2], the complex mol­ecules are located on a crystallographic twofold rotation axis and the CdII ion is octa­hedrally coordinated by two chelating 2,2′-bipyridine ligands and two O atoms from the carboxyl­ate groups of two 2-(benzimidazol-2-ylsulfan­yl)acetate ligands. The two carboxyl­ate ligands adopt a cis configuration with respect to each other. Within each of these ligands, the imidazole fragments are bent back in a loop towards the acetyl groups, forming intra­molecular N—H⋯O hydrogen bonds, which help to stablilize the mononuclear complex. Adjacent mol­ecules are further linked by weak C—H⋯O hydrogen bonds, resulting in a chain along the c axis

Linezolid and Rifampicin Combination to Combat cfr-Positive Multidrug-Resistant MRSA in Murine Models of Bacteremia and Skin and Skin Structure Infection.

Linezolid resistance mediated by the cfr gene in MRSA represents a global concern. We investigated relevant phenotype differences between cfr-positive and -negative MRSA that contribute to pathogenesis, and the efficacy of linezolid-based combination therapies in murine models of bacteremia and skin and skin structure infection (SSSI). As a group, cfr-positive MRSA exhibited significantly reduced susceptibilities to the host defense peptides tPMPs, human neutrophil peptide-1 (hNP-1), and cathelicidin LL-37 (P &lt; 0.01). In addition, increased binding to fibronectin (FN) and endothelial cells paralleled robust biofilm formation in cfr-positive vs. -negative MRSA. In vitro phenotypes of cfr-positive MRSA translated into poor outcomes of linezolid monotherapy in vivo in murine bacteremia and SSSI models. Importantly, rifampicin showed synergistic activity as a combinatorial partner with linezolid, and the EC50 of linezolid decreased 6-fold in the presence of rifampicin. Furthermore, this combination therapy displayed efficacy against cfr-positive MRSA at clinically relevant doses. Altogether, these data suggest that the use of linezolid in combination with rifampicin poses a viable therapeutic alternative for bacteremia and SSSI caused by cfr-positive multidrug resistant MRSA

catena-Poly[[(1,10-phenanthroline)cadmium(II)]-μ-2-(1,3-benzimidazol-2-ylsulfan­yl)acetato-κ3 N 1,O:N 3]

In title compound, [Cd(C9H6N2O2S)(C12H8N2)]n, the CdII atom is in a distorted tetra­gonal-pyramidal environment, coordinated by one chelating 1,10-phenanthroline ligand, one chelating 2-(1,3-benzimidazol-2-ylsulfan­yl)acetate (bia) ligand bound through one N atom and one O atom of the carboxyl group, and one N atom from a second bia ligand. Each bia ligand acts as bridge between CdII ions, forming one-dimensional coordination polymers along [010], with a shortest Cd⋯Cd distance of 4.27 (2) Å

(Ethyl­enediamine-κ2 N,N′)bis­[3-(2-pyridyl)-5-(4-pyrid­yl)-1,2,4-triazolato-κ2 N 2,N 3]zinc(II) methanol solvate dihydrate

The asymmetric unit of the title compound, [Zn(C12H8N5)2(C2H8N2)]·CH3OH·2H2O, contains a ZnII cation, octahedrally coordinated by two 3-(2-pyrid­yl)-5-(4-pyrid­yl)-1,2,4-triazolate anions, a chelating ethane-1,2-diamine mol­ecule, a methanol solvent mol­ecule, and two crystal water mol­ecules. In the crystal packing, complex mol­ecules are linked by hydrogen bonds into a two-dimensional layer

Molecular mechanism of fluoroquinolones resistance in Mycoplasma hominis clinical isolates

To evaluate the molecular mechanism of fluoroquinolones resistance in Mycoplasma hominis (MH) clinical strains isolated from urogenital specimens. 15 MH clinical isolates with different phenotypes of resistance to fluoroquinolones antibiotics were screened for mutations in the quinolone resistance-determining regions (QRDRs) of DNA gyrase (gyrA and gyrB) and topoisomerase IV (parC and parE) in comparison with the reference strain PG21, which is susceptible to fluoroquinolones antibiotics. 15 MH isolates with three kinds of quinolone resistance phenotypes were obtained. Thirteen out of these quinolone-resistant isolates were found to carry nucleotide substitutions in either gyrA or parC. There were no alterations in gyrB and no mutations were found in the isolates with a phenotype of resistance to Ofloxacin (OFX), intermediate resistant to Levofloxacin (LVX) and Sparfloxacin (SFX), and those susceptible to all three tested antibiotics. The molecular mechanism of fluoroquinolone resistance in clinical isolates of MH was reported in this study. The single amino acid mutation in ParC of MH may relate to the resistance to OFX and LVX and the high-level resistance to fluoroquinolones for MH is likely associated with mutations in both DNA gyrase and the ParC subunit of topoisomerase IV