Synthesis, anticancer and antibacterial activity of some novel mononuclear Ru(II) complexes

In search of potential anticancer drug candidates in ruthenium complexes, a series of mononuclear ruthenium complexes of the type [Ru(phen)(2)(nmit)]Cl(2) (Ru1), [Ru(bpy)(2)(nmit)]Cl(2) (Ru2), [Ru(phen)(2)(icpl)]Cl(2) (Ru3), Ru(bpy)(2)(icpl)]Cl(2) (Ru4) (phen=1,10-phenanthroline; bpy=2,2'-bipyridine; nmit=N-methyl-isatin-3-thiosemicarbazone, icpl=isatin-3-(4-Cl-phenyl)thiosemicarbazone) and [Ru(phen)(2)(aze)]Cl(2) (Ru5), [Ru(bpy)(2)(aze)]Cl(2) (Ru6) (aze=acetazolamide) and [Ru(phen)(2)(R-tsc)](ClO(4))(2) (R=methyl (Ru7), ethyl (Ru8), cyclohexyl (Ru9), 4-Cl-phenyl (10), 4-Br-phenyl (Ru11), and 4-EtO-phenyl (Ru12), tsc=thiosemicarbazone) were prepared and characterized by elemental analysis, FTIR, (1)H-NMR and FAB-MS. Effect of these complexes on the growth of a transplantable murine tumor cell line (Ehrlich Ascites Carcinoma) and their antibacterial activity were studied. In cancer study the effect of hematological profile of the tumor hosts have also been studied. In the cancer study, the complexes Ru1-Ru4, Ru10 and Ru11 have remarkably decreased the tumor volume and viable ascitic cell count as indicated by trypan blue dye exclusion test (p<0.05). Treatment with the ruthenium complexes prolonged the lifespan of Ehrlich Ascites Carcinoma (EAC) bearing mice. Tumor inhibition by the ruthenium chelates was followed by improvements in hemoglobin, RBC and WBC values. All the complexes showed antibacterial activity, except Ru5 and Ru6. Thus, the results suggest that these ruthenium complexes have significant antitumor property and antibacterial activity. The results also reflect that the drug does not adversely affect the hematological profiles as compared to that of cisplatin on the host.     

Thermophilic laccase from xerophyte species Opuntia vulgaris

Two laccase temperature isoforms capable of oxidizing phenolic compounds to quinones were isolated and purified to homogeneity from the cladodes of the xerophyte species Opuntia vulgaris. These catalytically active proteins exhibit apparent molecular masses of 137 and 90 kDa. Under reducing conditions, both isoforms yielded a subunit molecular mass of 43 kDa, suggesting that the enzyme is a multimer of the 43 kDa subunit. The 137 kDa isoform when heated at 80°C for 3min generated three polypeptide bands on activity stained polyacrylamide gels exhibiting 137, 90 and 43 kDa molecular forms. All isoforms of the enzyme exhibited an optimum pH of 10 when 2,6‐dimethoxyphenol was used as a substrate. The optimum temperature of the 137 kDa enzyme form was noted to be 80°C and that of the 90 kDa enzyme form was 70°C. Denaturation kinetics of both the laccase isoforms carried out at their respective optimum temperatures for 30 min exhibited enzyme activity in excess of their t_1/2 values throughout the assay period. The K_m for the 137 kDa form was determined to be 2.2 ± 0.3 mm and the V_max was 2.8 ± 0.2 IU/mL. These high temperature stable laccase isoforms having alkaline pH optima can find significant industrial use. Copyright © 2010 John Wiley & Sons, Ltd.     

Synthesis of the Upstream Terminal Disaccharide of the O-Antigenic Polysaccharide of Vibrio cholerae O37

The terminal disaccharide of the O-antigenic polysaccharide of Vibrio cholerae O37, 4-O-methyl-α-D-QuiNAc-(1→4)-α-d-QuiNAc, was synthesized as methyl glycoside involving glycosylation between glycosyl donor ethyl 2-azido-3-O-benzyl-2,6-dideoxy-4-O-methyl-6-iodo-1-thio-α-d-glucopyranoside and glycosyl acceptor methyl 2-azido-3-O-benzyl-2,6-dideoxy-6-iodo-α-d-glucopyranoside. Dehalogenation, global deprotection, and reduction of the azide to amine were effected in one step by catalytic hydrogenation. It was followed by selective N-acetylation to give the desired deprotected disaccharide.     

Polymerization of Acrylonitrile with Ceric lon-2-Propanethiol as Initiator System

The kinetics of the polymerization of arylonitrile with ceric ammonium sulfate in the presence of 2-propanethiol as the redox initiator system in aqueous solution has been investigated. The rate of polymerization was found to be proportional to the square root of both ceric ion and thiol concentrations, and the monomer exponent was close to 1.5. Spectral studies indicated that there is a complex formation between ceric ion and the monomer acrylonitrile. A kinetic scheme, based on initial formation of this complex and its subsequent reaction with the thiol to produce the free radicals (RS.) responsible for initiation has been postulated to account for the observed results. The activation energy and different kinetic and transfer constants for the system have also been evaluated.     

Biophysical characterization of thermophilic laccase from the xerophytes: Cereus pterogonus and Opuntia vulgaris

Biophysical characterization of laccase enzyme isoforms from two different xerophytic plants Cereus pterogonus and Opuntia vulgaris was carried out using EPR, fluorescence and circular dichroism (CD) spectroscopy while their thermal denaturation profiles were investigated employing differential scanning calorimetry (DSC) and thermogravimetric analysis (TGA). EPR analysis revealed the presence of endogenous copper. The hyperfine splitting of EPR spectrum reduced with increase in the complexity of enzyme protein. Raise in temperature did not alter the protein fluorescence emission suggestive of high temperature stability of the enzyme, causing the tryptophan and tyrosine residues to remain buried within the protein structure. Far-UV CD spectrum revealed existence of 60 % random coils in enzyme structure even at elevated temperatures and in presence of metal ions and protein denaturants. DSC analysis provided a Tm in the range 95–121 °C for the native and 158–199 °C for the metal associated laccase isoforms. Loss in weight of the enzyme protein by 10–18 % was noted up to 100 °C when determined through TGA. The thermostable plant xerophytic laccase enzyme isoforms will be of potential use in textile, dyeing, pulping and biotechnology applications.     

Protein-assisted synthesis route of metal nanoparticles: exploration of key chemistry of the biomolecule

Abstract  

Essentially, biomolecule assisted synthesis of inorganic nanoparticles can be divided into two categories. One uses multi-domain protein cages (template) and other relies on the self-assembly of the biomolecules including small peptides, DNA, and denatured protein. Protein templated synthesis of various nanomaterials is relatively well understood as the cages of the biological macromolecules and their specific interaction with inorganic ions ultimately dictate the size and crystallinity of the nanomaterials. On the other hand formation of nanoparticles using protein in the cost of the native structural integrity for the self-assembly is not well understood till date. In the present work we report a protein-assisted synthesis route to prepare highly crystalline 3–5 nm gold nanoparticles, which relies systematic thermal denaturation of a number of proteins and protein mixture from Escherichia coli in absence of any reducing agent. By using UV–vis, circular dichroism spectroscopy, and high-resolution transmission electron microscopy we have explored details of the associated biochemistry of the proteins dictating kinetics, size, and crystallinity of the nanoparticles. The kinetics of nanoparticles formation in this route, which is sigmoidal in nature, has been modelled in a simple scheme of autocatalytic process. Interestingly, the protein-capped as prepared Au nanoparticles are found to serve as effective catalyst to activate the reduction of 4-nitrophenol in the presence of NaBH₄. The kinetic data obtained by monitoring the reduction of 4-nitrophenol by UV/vis-spectroscopy revealing the efficient catalytic activity of the nanoparticles have been explained in terms of the Langmuir–Hinshelwood model. The methodology and the details of the protein chemistry presented here may find relevance in the protein-assisted synthesis of inorganic nanostructures in general.     

Interacting three fluid system and thermodynamics of the universe bounded by the event horizon

The work deals with the thermodynamics of the universe bounded by the event horizon. The matter in the universe has three constituents namely dark energy, dark matter and radiation in nature and interaction between then is assumed. The variation of entropy of the surface of the horizon is obtained from unified first law while matter entropy variation is calculated from the Gibbss’ law. Finally, validity of the generalized second law of thermodynamics is examined and conclusions are written point wise.     

Role of impurity influenced domain on excitation profile of doped quantum dot subject to oscillatory confinement potential

We explore the excitation profile of a repulsive impurity doped quantum dot under a periodically fluctuating confinement potential. We have considered Gaussian impurity centers. The investigation points to a minimum value of spatial extension of impurity domain below which significant excitation is not feasible. In general, excitation becomes maximum at some typical value of impurity strength depending upon the location and the spatial stretch of the dopant. The rate of transition to the excited states depends on the above spatial stretch which gets modulated by the oscillating confinement potential and explains the excitation maximization quite elegantly.     

A naphthyridine based macrocyclic “switching on” fluorescent receptor for cadmium

A new macrocyclic receptor 1 having [1,8]-naphthyridine fluorophore is designed and synthesized for selective fluorescence sensing of Cd²⁺. Receptor 1 selectively responds to Cd²⁺ over other tested metal ions via a large enhancement of emission intensity due to the cation-induced CHEF (chelation enhanced fluorescence) effect. Receptor 1 although exhibits some affinity towards Zn²⁺, it selectively binds Cd²⁺ over Zn²⁺. Binding and selectivity were examined by ¹H-NMR, fluorescence, UV-vis, mass and IR-spectroscopic techniques.     

Multi-component catalysts with spinel structure for the selective reduction of nitrogen oxide by ethylene in lean-exhaust gas streams

The Ga₂O₃-Al₂O₃-ZnO (GAZ) multi-component spinel powders with incorporated Cu²⁺, Co²⁺, Fe²⁺, Ni²⁺, Mn²⁺ and In²⁺ metal cations were synthesized by co-precipitation method from a mixed solution of nitrate salts. Spinel crystal structure of each composition was confirmed by XRD measurements. The multi-component oxide powders were tested in the reduction of nitrogen oxide (NO) under lean conditions. Among the catalysts tested, In₂O₃-containing GAZ with a pure spinel phase structure showed promising catalytic activity in the NO reduction in the presence of 10% H₂O vapor. In addition, the effect of H₂O vapor and SO₂ on the selective reduction of NO over In₂O₃-GAZ/cordierite and In₂O₃-GAZ/metal honeycombs catalysts has been investigated.