Rat Liver Mitochondrial Dysfunction Induced by an Organic Arsenical Compound 4-(2-Nitrobenzaliminyl) Phenyl Arsenoxide.

Arsenic is successfully used in cancer chemotherapy and several cancer treatments on account of its apoptogenic effects. However, it is environmentally hazardous with potential for toxicity when distributed in the soil, water, and food, and long exposure to water contaminated with Arsenic may induce cancers. Some research studies have reported that liver is the storage site and an important target organ for Arsenic toxicity. In the present work, a new kind of organic arsenic compound, 4-(2-nitrobenzaliminyl) phenyl arsenoxide (NPA), was synthesized, and its potential involvement of mitochondria was explored. The results presented that the toxicology of NPA, at least in part, mediated mitochondrial function and may thoroughly destroy mitochondrial membrane physiological functions. NPA induced mitochondrial permeability transition pore (mtPTP) opening that induces mitochondrial biochemical abnormalities as evidenced by mitochondrial swelling, mitochondrial membrane potential breakdown, membrane fluidity alterations, and the strikingly remarkable protection of CsA. Meanwhile, both the decreased respiration rate of state 4 and the increased inner membrane H(+) permeabilization revealed that the inner membrane function regarding important energy production chain was destroyed. The toxicity of NPA is due to its interaction with mitochondrial membrane thiol protein. This conclusion is based on the protective effects of RR, DTT, and MBM(+).

3-(2-Amino-ethyl)-2-anilinoquinazolin-4(3H)-one methanol hemisolvate.

The title methanol hemisolvated quinazolin-(3H)-one, C(16)H(16)N(4)O·0.5CH(3)OH, has an anilino substituent in the 2-position and an amino-ethyl substituent in the 3-position of the planar fused-ring system (r.m.s. deviation = 0.019 Å). The anilino N atom donates an intramolecular hydrogen bond to the amino-ethyl N atom. The mol-ecule and the solvent methanol mol-ecule are linked by N-H⋯N, N-H⋯O and O-H⋯O hydrogen bonds. The methanol mol-ecule is disordered over two equally occupied positions about a twofold rotation axis.

2-(4-Fluoro-anilino)-3-(2-hydroxy-ethyl)quinazolin-4(3H)-one.

The mol-ecular and crystal structures of the title compound, C(16)H(14)FN(3)O(2), are stabilized by intra-molecular N-H⋯O and inter-molecular O-H⋯O hydrogen bonds. The existence of non-classical intra-molecular C-H⋯N hydrogen bonds provides a dihedral angle between the fluoro-substituted benzene and pyrimidinone rings of 7.9 (1)°.

Ethyl 3-amino-1-phenyl-1H-benzo[f]chromene-2-carboxyl-ate.

The pyranyl ring of the title compound, C(22)H(19)NO(3), adopts a flattened-boat conformation. The dihedral angle between naphthalene and phenyl rings is 78.3 (1)°The mol-ecule also features an intra-molecular N-H⋯O(carbon-yl) hydrogen bond. Adjacent mol-ecules are linked by an inter-molecular N-H⋯O(carbon-yl) hydrogen bond, forming a zigzag chain that runs along the c axis.

Synthesis of a novel p-hydroxycinnamic amide with anticancer capability and its interaction with human serum albumin.

In the present study, a novel p-hydroxycinnamic amide (E)-3-(4-hydroxyphenyl)-N-(4-(N-(5-meth oxypyrimidin-2-yl)-sulfamoyl)phenyl)acrylamide (HMSP) was synthesized and confirmed. In vitro cytotoxic assays indicated that HMSP was able to inhibit the proliferation of various cancer cell lines. The interaction between HMSP and human serum albumin (HSA) was examined by fluorescence, UV-Vis and circular dichroism (CD) spectra, in addition to molecular simulation. The fluorescence and UV-Vis spectra data indicated that the binding of HMSP with HSA was a static process. According to the fluorescence quenching calculation, the corresponding thermodynamic parameters, bimolecular quenching rate constant and apparent quenching constants were calculated. Van der Walls forces and hydrogen bonds were vital in the binding of HMSP on HSA. The distances between HSA and its derivatives were obtained. Furthermore, competitive experiments and molecular modeling results suggested that the binding of the compound on HSA mainly occurred in site I (sub-domain IIA). Changes in HSA conformation were observed from synchronous fluorescence and CD spectra, which were further investigated by molecular dynamic simulations.