The chemical properties of alicyclic heterocycles are similar to those of the corresponding chain compounds. Compound: 2-Furoic hydrazide, is researched, Molecular C5H6N2O2, CAS is 3326-71-4, about Chemistry of mixed-ligand oxidovanadium(IV) complexes of aroylhydrazones incorporating quinoline derivatives: Study of solution behavior, theoretical evaluation and protein/DNA interaction, the main research direction is preparation oxidovanadium Schiff base aroylhydrazone quinoline derivative complex; crystal mol structure oxidovanadium Schiff aroylhydrazone quinoline derivative complex; cyclic voltammetry oxidovanadium Schiff base aroylhydrazone quinoline derivative complex; EPR spectra oxidovanadium Schiff base aroylhydrazone quinoline derivative complex; DNA interaction oxidovanadium Schiff base aroylhydrazone quinoline derivative complex; Aroylhydrazone; DFT calculations; DNA binding; Mixed-ligand oxidovanadium(IV); Protein interaction.Name: 2-Furoic hydrazide.
A series of eight hexacoordinated mixed-ligand oxidovanadium(IV) complexes [VO(Lx)(LN-N)] (1-8), where Lx = L1 – L4 are four differently substituted ONO donor aroylhydrazone ligands and LN-N are N,N-donor bases like 2,2′-bipyridine (bipy) (1, 3, 5 and 7) and 1,10-phenanthroline (phen) (2, 4, 6 and 8), are reported. All synthesized complexes were characterized by various physicochem. techniques and mol. structures of 1 and 6 were determined by x-ray crystallog. With a view to evaluate the biol. activity of the VIVO species, the behavior of the systems VIVO2+/Lx, VIVO2+/Lx/bipy and VIVO2+/Lx/phen was studied as a function of pH in a mixture of H2O/DMSO 50/50 (volume/volume). DFT calculations allowed finding out the relative stability of the tautomeric forms of the ligands, and predicting the structure of vanadium complexes and their EPR parameters. To study their interaction with proteins, firstly the ternary systems VIVO2+/L1,2 with 1-methylimidazole, which is a good model for histidine binding, were examined Subsequently the interaction of the complexes with lysozyme (Lyz), cytochrome c (Cyt) and bovine serum albumin (BSA) was studied. The complexes showed moderate binding affinity towards BSA, while no interaction takes place with lysozyme and cytochrome c. This could be explained with the higher number of accessible coordinating and polar residues for BSA than for Lyz and Cyt. Further, the complexes were also evaluated for their DNA binding propensity through UV-visible absorption titration and fluorescence spectral studies. These results were consistent with BSA binding affinity and showed moderate binding affinity towards CT-DNA.
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Reference:
Benzisoxazole – Wikipedia,
Benzisoxazole – an overview | ScienceDirect Topics