Metal complexes of triazole-2-yl thiourea: synthesis, characterization and equilibrium studies

Triazoles have been reported to be biologically versatile compounds, having bactericidal[1], fungicidal [2] insecticidal[3] and pesticidal[4]properties, also thiourea. Frequently display a wide biocidal activities [5,6]. It is well known that certain metal complexes have greater activity than the coordinating agents themselves [7] This has led us to study in the present work a new thiourea derivative having a triazole moiety with some transition metal ions, in continuation to previous studies on thiourea complexes[8]. The present investigation comprises l-triazole-2-yl-3-benzoyl- thiourea, BTu, and some of its metal complexes. The composition and structure of the formed complexes have been characterized by elemental analysis, potentiometric titrations, electrolyte conductance, IR, electronic and proton NMR spectrometry and magnetic susceptibility measurements

Effect of acid amides on porcine pepsin

The activity of porcine pepsin toward a synthetic peptide was examined kinetically in presence and absence of some acid amides which are mainly urea analogues The peptide Ac-ILe-Glu phe[No2] -Argamide [assigned peptide VIR] was synthesized to fit the subsites S2 and S3 of porcine pepsin. This peptide was purfied before its use in the assays However, it was found that urea has no effect on k[cat] value of the enzyme while acetamide effect showed its elevation. On the other hand, thiourea acted as a reversible inhibitor which was a noncompetitive type. Also, N.N-diphenyl thiourea showed a reversible inhibition. These data suggested that hydrogen binding and hydrophobic interactions affect the subsites and both thiourea and N,N-diphenyl thiourea may modify one of the subsites through C= S group