Synthesis and Cytotoxic Activity of Novel Pyrazoline Derivatives against Human Lung Tumor Cell Line (A549)

In the present investigation, a series of 5‐(‐4‐(substituted)phenyl)‐3‐(4‐hydroxy‐3‐methylphenyl)‐4,5‐dihydro‐1H‐1‐pyrazolyl‐2‐toluidino methane thione and 5‐(substituted)phenyl‐3‐(4‐hydroxy‐3‐methylphenyl)‐4,5‐dihydro‐1H‐1‐pyrazolyl‐2‐methoxy anilino methane thiones were synthesized and were examined against human lung tumor cell line (A549) in vitro using the MTT assay system. Among those tested, 5‐(4‐flurophenyl)‐3‐(4‐hydroxy‐3‐methylphenyl)‐4,5‐dihydro‐1H‐1‐pyrazolyl‐2‐toluidino methane thione & 5‐(4‐chlorophenyl)‐3‐(4‐hydroxy‐3‐methylphenyl)‐4,5‐dihydro‐1H‐1‐pyrazolyl‐2‐methoxy anilino methane thione showed more potent cytotoxicity against human lung tumor cell line (A549) than the other synthesized compounds.     

Intramolecular van der Waals Interactions Challenge Anion Binding in perthio-Bambusurils

Bambusurils (BUs) are known to be rigid cavitands that feature an extended, jigger-like conformation, and the BU[6]s strongly bind anions within their hydrophobic cavity. These features are not necessarily shared by the family of perthio-BUs. This study reveals that perthio-BUs assume a compact conformation and perthio-BU[6]s are poor anion binders, crystallizing as anion-free species from solutions containing halide salts. Computational studies show that the equatorial sulfur atoms compete against guest anions for binding with the glycoluril methine groups via strong van der Waals (vdW) attractive interactions. These competitive contacts not only account for the diminished anion-binding of perthio-BUs, but also explain their compact conformation. The semithio- and perthio-BU[4]s form linear coordination polymers with Hg^II in the solid-state regardless of their intrinsic molecular conformation. The strong involvement of sulfur atoms in intramolecular interactions differentiates the equatorial from the axial (peripheral) heteroatoms, thus offering chemoselective and regioselective transformations.     

Switchable Cucurbituril–Bipyridine Beacons

4‐Aminobipyridine derivatives form strong inclusion complexes with cucurbit[6]uril, exhibiting remarkably large enhancements in fluorescence intensity and quantum yields. The remarkable complexation‐induced pK_a shift (ΔpK_a=3.3) highlights the strong charge–dipole interaction upon binding. The reversible binding phenomenon can be used for the design of switchable beacons that can be incorporated into cascades of binding networks. This concept is demonstrated herein by three different applications: 1) a switchable fluorescent beacon for chemical sensing of transition metals and other ligands; 2) direct measurement of binding constants between cucurbit[6]uril and various nonfluorescent guest molecules; and 3) quantitative monitoring of biocatalytic reactions and determination of their kinetic parameters. The latter application is illustrated by the hydrolysis of an amide catalyzed by penicillin G acylase and by the elimination reaction of a β‐cabamoyloxy ketone catalyzed by aldolase antibody 38C2.     

Relaxation dynamics of charged gravitational collapse

We study analytically the relaxation dynamics of charged test fields left outside a newly born charged black hole. In particular, we obtain a simple analytic expression for the fundamental quasinormal resonances of near-extremal Reissner-Nordström black holes. The formula is expressed in terms of the black-hole physical parameters: , where TBH and Φ are the temperature and electric potential of the black hole, and q is the charge of the field.     

Understanding the enzymatic activity of 4-oxalocrotonate tautomerase and its mutant analogues: a computational study

The effect of replacing arginine residues (Arg) with citrulline residues (Cit) in the binding site of 4-oxalocrotonate tautomerase (4-OT) was investigated with force field molecular dynamics and hybrid quantum mechanics/molecular mechanics studies. It is found that the Arg61Cit mutation has only minor effects on the k(cat) and K(M) values determined experimentally because of the flexibility of this residue. The decrease in k(cat) and increase in K(M) for the Arg11Cit and Arg39Cit mutations are due to the disruption of the binding site, which arises from repulsive interactions with neighboring residues. The results of this investigation shed new light on the effects of mutations in the binding site of 4-OT and consequently on how the enzyme binds the active substrate.