New VIVO-complexes for oxidative desulfurization of refractory sulfur compounds in fuel: synthesis, structure, reactivity trend and mechanistic studies.

A series of 5-coordinate oxidovanadium(iv) complexes based on 2-(2'-hydroxyphenyl)imidazole (HPIMH), with substituent groups of different electronegativities on the phenolic para position (HPIMX; X = -H, -Br, -OMe and -NO2), were synthesized and characterized. Three of these complexes were characterized by single crystal X-ray diffraction, [VIVO(PIMH)2], [VIVO(PIMBr)2] and [VIVO(PIMNO2)2], as well as a dioxidovanadium(v) compound ([VVO2(PIMH)(PIMH2)]). The complexes were tested for their catalytic activities in the oxidation of dibenzothiophene (DBT), the major refractory organosulfur compound found in fuel. The nitro substituted compound [VIVO(PIMNO2)2] had the highest catalytic oxidation activity followed by: [VIVO(PIMH)2] > [VIVO(PIMBr)2] > [VIVO(PIMMeO)2]. The decrease in activity is attributed to the different electronegativities of the substituent groups, which influence the electron density on the metal center, the V[double bond, length as m-dash]O bond distances and infrared stretching bands. Geometry index (τ) values calculated from single crystal X-ray diffraction (SC-XRD) data and DFT studies provided further insights on the trend in activity observed. SC-XRD, EPR, 51V NMR and UV-Vis spectroscopies, and DFT studies were instrumental in studying the mechanism of the catalyzed reaction and proposal of intermediate species. Both radical and non-radical pathways are plausible for the catalytic oxidation and participation of reactive oxygen species in both pathways is also postulated.

Interaction and lipid-induced conformation of two cecropin-melittin hybrid peptides depend on peptide and membrane composition.

The interaction of two hybrid peptides of cecropin A and melittin [CA(1-8)M(1-18) and CA(1-7)M(2-9)] with liposomes was studied by differential scanning calorimetry (DSC), circular dichroism (CD), and quasi-elastic light scattering (QELS). The study was carried out with large unilamellar vesicles (LUVs) of three different lipid compositions: 1,2-dimyristoil-sn-glycero-3-phosphocholine (DMPC), 1,2-dimyristoyl-sn-glycero-3-phospho-rac-(1-glycerol) (DMPG) and a binary mixture of DMPC/DMPG, in a wide range of peptide-to-lipid (P:L) molar ratios (0 to 1:7). DSC results indicate that, for both peptides, the interaction depends on membrane composition, with very different behavior for zwitterionic and anionic membranes. CD data show that, although the two peptides have different secondary structures in buffer (random coil for CA(1-7)M(2-9) and predominantly beta-sheet for CA(1-8)M(1-18)), they both adopt an alpha-helical structure in the presence of the membranes. Overall, results are compatible with a model involving a strong electrostatic surface interaction between the peptides and the negatively charged liposomes, which gives place to aggregation in the gel phase and precipitation after a threshold peptide concentration. In the case of zwitterionic membranes, a progressive surface coverage with peptide molecules destabilizes the membrane, eventually leading to membrane disruption. Moreover, delicate modulations in behavior were observed depending on the peptide.