7-(4-Chlorophenyl)-1-hydroxy-5-methylpyrido[3,4-d]pyridazin-4(3H)-one: synthesis, solvatomorphism, in vitro anti-inflammatory and cytotoxic activity studies and in silico analysis.

The newly obtained compound 7-(4-chlorophenyl)-1-hydroxy-5-methylpyrido[3,4-d]pyridazin-4(3H)-one (CPM) was crystallized as two new variable solvates, namely, the dimethyl sulfoxide monosolvate, CHClNO·CHSO (I), and the sesquisolvate, CHClNO·1.5CHSO (II), and their structures were confirmed by single-crystal X-ray diffraction analysis. In previous work, 1-hydroxy-5-methyl-7-phenylpyrido[3,4-d]pyridazin-4(3H)-one (PM) was found to display anticancer activity.

Pyrimidine Schiff Bases: Synthesis, Structural Characterization and Recent Studies on Biological Activities.

Recently, 5-[(4-ethoxyphenyl)imino]methyl-N-(4-fluorophenyl)-6-methyl-2-phenylpyrimidin-4-amine has been synthesized, characterized, and evaluated for its antibacterial activity against in combination with antineoplastic activity against gastric adenocarcinoma. In this study, new 5-iminomethylpyrimidine compounds were synthesized which differ in the substituent(s) of the aromatic ring attached to the imine group. The structures of newly obtained pyrimidine Schiff bases were established by spectroscopy techniques (ESI-MS, FTIR and H NMR).

Highly regioselective and diastereoselective synthesis of novel pyrazinoindolones a base-mediated Ugi--alkylation sequence.

An efficient base-mediated/metal-free approach has been developed for the synthesis of 1-oxo-1,2,3,4-tetrahydropyrazino[1,2-]indole-3-carboxamide derivatives intramolecular indole N-H alkylation of novel bis-amide Ugi-adducts. In this protocol the Ugi reaction of ()-cinnamaldehyde derivatives, 2-chloroaniline, indole-2-carboxylic acid and different isocyanides was designed for the preparation of bis-amides. The main highlight of this study is the practical and highly regioselective preparation of new polycyclic functionalized pyrazino derivatives.

Structure and cytotoxic properties of 1-hydroxy-5-methyl-7-phenylpyrido[3,4-d]pyridazin-4(3H)-one and its mono- and disubstituted ethyl acetates.

Derivatives of pyrido[3,4-d]pyridazine, namely, 1-hydroxy-5-methyl-7-phenylpyrido[3,4-d]pyridazin-4(3H)-one dimethylformamide monosolvate, CHNO·CHNO (2), ethyl [1-(2-ethoxy-2-oxoethoxy)-5-methyl-4-oxo-7-phenyl-3,4-dihydropyrido[3,4-d]pyridazin-3-yl]acetate, CHNO (3), and ethyl [(5-methyl-4-oxo-7-phenyl-3,4-dihydropyrido[3,4-d]pyridazin-1-yl)oxy]acetate, CHNO (4), were synthesized with the aim of discovering new potential biologically active agents. The properties of all three derivatives were characterized by H NMR, C NMR and FT-IR spectroscopic analysis. All the crystals were obtained by a solvent diffusion method from dimethylformamide (DMF) or dimethyl sulfoxide (DMSO) and characterized by single-crystal X-ray diffraction.

Synthesis, Structural Characterization and Anticancer Activity of New 5-Trifluoromethyl-2-thioxo-thiazolo[4,5-]pyrimidine Derivatives.

Thiazolo[4,5-]pyrimidine derivatives are considered potential therapeutic agents, particularly in the development of anticancer drugs. In this study, new 7-oxo-(), 7-chloro-() and also three 7-amino-() 5-trifluoromethyl-2-thioxo-thiazolo[4,5-]pyrimidine derivatives have been synthesized and evaluated for their potential anticancer activity. These derivatives were characterized by spectroscopic methods and elemental analysis, and the single-crystal X-ray diffraction was further performed to confirm a 3D structure for compounds and .

φYeO3-12 phage tail fiber Gp17 as a promising high specific tool for recognition of Yersinia enterocolitica pathogenic serotype O:3.

Yersiniosis is an infectious zoonotic disease caused by two enteropathogenic species of Gram-negative genus Yersinia: Yersinia enterocolitica and Yersinia pseudotuberculosis. Pigs and other wild and domestic animals are reservoirs for these bacteria. Infection is usually spread to humans by ingestion of contaminated food.

Synthesis, Crystal Structure, and Biological Evaluation of Novel 5-Hydroxymethylpyrimidines.

Pyrimidine displays a wide array of bioactivities, and thence, it is still considered a potent unit of new drug research. Its derivative, 5-hydroxymethylpyrimidine, can be found as a scaffold of nontypical nitrogen bases in DNA and as a core of some natural bioactive compounds. In this study, we obtained a series of 5-hydroxymethylpyrimidines that vary in the 4-position by the reduction of proper esters.

New Insights on the Feature and Function of Tail Tubular Protein B and Tail Fiber Protein of the Lytic Bacteriophage φYeO3-12 Specific for Serotype O:3.

For the first time, we are introducing TTPBgp12 and TFPgp17 as new members of the tail tubular proteins B (TTPB) and tail fiber proteins (TFP) family, respectively. These proteins originate from phage φYeO3-12. It was originally thought that these were structural proteins.

Synthesis and Biological Activity of New 7-Amino-oxazolo[5,4-]Pyrimidine Derivatives.

The synthesis of a series of novel 7-aminooxazolo[5,4-]pyrimidines , transformations during their synthesis and their physicochemical characteristics have been described. Complete detailed spectral analysis of the intermediates -, the -cyanooxazolylacetamidine by-products and final compounds has been carried out using MS, IR, 1D and 2D NMR spectroscopy. Theoretical research was carried out to explain the privileged formation of 7-aminooxazolo[5,4-]pyrimidines in relation to the possibility of their isomer formation and the related thermodynamic aspects.

Biochemical features of the novel Tail Tubular Protein A of Yersinia phage phiYeO3-12.

Tail Tubular Protein A (TTPA) was long thought to be strictly a structural protein of environmental bacteriophages. However, our recent work has suggested that some TTPAs have additional functional features and thus are dual-function proteins. This study introduces a new TTPA family member, TTPAgp11, which belongs to Yersinia phage phiYeO3-12.

Hydrolytic activity determination of Tail Tubular Protein A of Klebsiella pneumoniae bacteriophages towards saccharide substrates.

In this paper, the enzymatic activity, substrate specificity and antibiofilm feature of bacteriophage dual-function tail proteins are presented. So far, tail tubular proteins A-TTPAgp31 and TTPAgp44-have been considered as structural proteins of Klebsiella pneumoniae bacteriophages KP32 and KP34, respectively. Our results show that TTPAgp31 is able to hydrolyze maltose as well as Red-starch.