A simple and selective kinetic spectrophotometric method for the determination of kanamycin using acetylacetone-formaldehyde reagent in N,N′-dimethylformamide medium

A simple, sensitive, and selective kinetic spectrophotometric method for the determination of kanamycin in pure form and pharmaceutical formulations is described. The method is based on the measurement of the intensity of the yellow chromogen formed by the reaction between kanamycin and acetylacetone-formaldehyde reagent in a N,N′-dimethyl formamide medium. The variable-time method was used to evaluate the rate of reaction of the colored chromogen formed at 410 nm. The reaction conditions were optimized and the calibration graph was found to be linear in the range 60–160 μg/mL. The results obtained by the developed and reference methods are in good agreement. Various statistical parameters were evaluated to establish the precision, accuracy, repeatability, and reproducibility of the proposed method. The text was submitted by the authors in English.     

Selective small molecule inhibitors of glycogen synthase kinase-3 modulate glycogen metabolism and gene transcription

BACKGROUND: Glycogen synthase kinase-3 (GSK-3) is a serine/threonine protein kinase, the activity of which is inhibited by a variety of extracellular stimuli including insulin, growth factors, cell specification factors and cell adhesion. Consequently, inhibition of GSK-3 activity has been proposed to play a role in the regulation of numerous signalling pathways that elicit pleiotropic cellular responses. This report describes the identification and characterisation of potent and selective small molecule inhibitors of GSK-3. RESULTS: SB-216763 and SB-415286 are structurally distinct maleimides that inhibit GSK-3alpha in vitro, with K(i)s of 9 nM and 31 nM respectively, in an ATP competitive manner. These compounds inhibited GSK-3beta with similar potency. However, neither compound significantly inhibited any member of a panel of 24 other protein kinases. Furthermore, treatment of cells with either compound stimulated responses characteristic of extracellular stimuli that are known to inhibit GSK-3 activity. Thus, SB-216763 and SB-415286 stimulated glycogen synthesis in human liver cells and induced expression of a beta-catenin-LEF/TCF regulated reporter gene in HEK293 cells. In both cases, compound treatment was demonstrated to inhibit cellular GSK-3 activity as assessed by activation of glycogen synthase, which is a direct target of this kinase. CONCLUSIONS: SB-216763 and SB-415286 are novel, potent and selective cell permeable inhibitors of GSK-3. Therefore, these compounds represent valuable pharmacological tools with which the role of GSK-3 in cellular signalling can be further elucidated. Furthermore, development of similar compounds may be of use therapeutically in disease states associated with elevated GSK-3 activity such as non-insulin dependent diabetes mellitus and neurodegenerative disease.     

Surface ligands in the imprinting and binding of molecularly imprinted cross-linked micelles

Molecular recognition in water is challenging but water-soluble molecularly imprinted nanoparticle (MINP) receptors were produced readily by double cross-linking of surfactant micelles in the presence of suitable template molecules. When the micellar surface was decorated with different polyhydroxylated ligands, significant interactions could be introduced between the surface ligands and the template. Flexible surface ligands worked better than rigid ones to interact with the polar moiety of the template, especially for those template molecules whose water-exposed surface is not properly solvated by water. The importance of these hydrophilic interactions was examined in the context of different substrates, density of the surface ligands, and surface-cross-linking density of the MINP. Together with the hydrophobic interactions in the core, the surface hydrophilic interactions can be used to enhance the binding of guest molecules in water.     

Large-xF spin asymmetry inπ0 production by 200-GeV polarized protons

The spin asymmetryA _N for inclusive ⁰ production by 200-GeV transversely-polarized protons on a liquid hydrogen target has been measured at Fermilab over a wide range ofx _F, with 0.5p _T<2 gev/c.=">x _F>0.3, the asymmetry rises with increasingx _F and reaches a value ofA _N=0.15±0.03 in the region 0.6x _F<0.8. this=" result=" provides=" new=" input=" regarding=" the=" question=" of=" the=" internal=" spin=" structure=" of=" transversely-polarized=">This work was performed at the Fermi National Accelerator Laboratory, which is operated by University Research Associates, Inc., under contract DE-AC02-76CH03000 with the U.S. Department of Energy. Work supported in part by the U.S. Department of Energy, Division of High Energy Physics, Contracts W-31-109-ENG-38, W-7405-ENG-36, DE-AC02-76ER02289, DE-AS05-76ER05096     

Search for the rare decay K(L)-->pi(0)e(+)e(-)

The KTeV/E799 experiment at Fermilab has searched for the rare kaon decay K(L)-->pi(0)e(+)e(-). This mode is expected to have a significant CP violating component. The measurement of its branching ratio could support the standard model or could indicate the existence of new physics. This Letter reports new results from the 1999-2000 data set. One event is observed with an expected background at 0.99+/-0.35 events. We set a limit on the branching ratio of 3.5x10(-10) at the 90% confidence level. Combining with the previous result based on the data set taken in 1997 yields the final KTeV result: BR(K(L)-->pi(0)e(+)e(-))<2.8x10(-10) at 90% C.L.     

Measurements of the decay KL-->e+ e- gamma

The E799-II (KTeV) experiment at Fermilab has collected 83 262 K(L)-->e+ e- gamma(gamma) events above a background of 79 events. We measure a decay width, normalized to the K(L)-->pi0pi0pi(D)0 (pi0-->gammagamma, pi0-->gammagamma, pi(D0-->e+ e- gamma(gamma)) decay width, of Gamma(K(L)-->e+e-gamma(gamma))/Gamma(K(L)-->pi0pi0pi(D)0)=(1.3302+/-0.0046(stat)+/-0.0102(syst)) x 10(-3). We also measure parameters of two K(L)gamma*gamma form factor models. In the Bergstr?m-Massó-Singer parametrization, we find Calpha(K*)= -0.517 +/- 0.030(stat) +/- 0.022(syst). We separately fit for the first parameter of the D'Ambrosio-Isidori-Portolés model and find alpha(DIP)= -1.729 +/- 0.043(stat) +/- 0.028(syst).