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Synthesis, SAR and molecular modelling studies of acylthiocarbamates and their parent thiocarbamates as potent non-nucleoside reverse transcriptase inhibitors related to PETT derivatives
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Preparation and characterization of water-soluble, not PAMAM-structured dendrimer prodrugs of an anti-HIV-1 O-TC derivative for in vivo and clinical applications.
No full textAssessing the chemical cross-reaction from cefixime and some non-steroidal anti-inflammatory agents in a soluble formulation
No full textThe presence of chemical cross-reactivity betwen drugs may be an underestimated factor, responsible for decreased bio-availability of a drug active component(s); the absence of chemical cross-reactivity between drugs is undoubtedly the prerequisite for their simultaneous co-administration. Here, by means of thin layer chromatography, we show that cefixime, a third generation oral cephalosporin, does not display chemical reactivity versus a series of non-steroidal antiinflammatory agents. The four compounds tested can therefore be safely soluted together with the cephalosporin
HIGHLY-FUNCTIONALIZED AMINO PYRAZOLES AS ANTIOXIDANT AGENTS: A PRELIMINARY SYNTHETIC ACCESSIBILITY STUDY
No full text5-pyrazolyl urea derivatives showed interesting pharmaceutical properties. In particular, compounds 1
(Figure 1) showed promising antioxidant activity by inhibiting ROS formation in platelet. The free amino
group on the pyrazole ring appear to be essential for the antioxidant activity whereas the substitution of
the catechol moiety (X group, Figure 1) modulate the ability of the compound to block ROS formation. To further extend the SARs of derivatives 1 and evaluate the effect on the activity of the introduction of a
N-phenyl substituent on the pyrazole scaffold, we planned the synthesis of new amino pyrazoles 2 (Figure
1). In order to assess the chemical accessibility to the desired compounds, synthetic path A and B (Scheme
1) were considered. Methylhydrazine and p-anisaldehyde were selected as template reagents. Despite literature data, path A proved to be ineffective as the cyclization reaction could not occur in a
number of different experimental conditions. Path B led to the isolation of the desired compound as a
mixture of the two possible N-methyl isomers in good yields. In the poster, the different synthetic
conditions as well as the characterization of the obtained pyrazole isomers will be presented
Human rhinovirus 3C protease: a cysteine protease showing the trypsin(ogen)-like fold
No full textViral-encoded proteases cleave precursor polyprotein(s) leading to maturation of infectious virions. Strikingly, human rhinovirus 3C protease shows the trypsin(ogen)-like serine protease fold based on two topologically equivalent six-stranded beta-barrels, but displays residue Cys147 as the active site nucleophile. By contrast, papain, which is representative of most cysteine proteases, does not display the trypsin(ogen)-like fold. Remarkably, in human rhinovirus 3C cysteine protease, the catalytic residues Cys147, His40 and Glu71 are positioned as Ser195, His57 and Aspl02, respectively, building up the catalytic triad of serine proteases in the chymotrypsin-trypsin-elastase family. However, as compared to trypsin-like serine proteases and their zymogens, residue His40 and the oxyanion hole of human rhinovirus 3C cysteine protease, both key structural components of the active site, are located closer to the protein core. Human rhinovirus 3C cysteine protease cleaves preferentially Gln-Gly peptide bonds or, less commonly, the Gln-Ser, Gln-Ala, Glu-Ser or Glu-Gly pairs. Finally, human rhinovirus 3C cysteine protease and the 3CD cysteine proteasepolymerase covalent complex bind the 5‘ non-coding region of rhinovirus genomic RNA, an essential function for replication of the viral genome
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