Characterization of the TiO2/dye/electrolyte interfaces in dye-sensitized solar cells by means of a titania-binding nitroxide.

Dye-sensitized solar cells (DSSCs) have been characterized in several literature examples by using relatively complex methods and/or modified DSSC conditions with respect to the usual working ones. In this study, we propose a method for the investigation of the interfaces TiO2/dye/electrolyte in a DSSC at its usual working conditions. This method implies the use of a computer-aided analysis of the electron paramagnetic resonance (EPR) spectra of the spin probe 4-carboxy-2,2,6,6-tetramethylpiperidine 1-oxyl (4-carboxy-TEMPO, indicated as 4-cT).

Anionic sulfonated and carboxylated PPI dendrimers with the EDA core: synthesis and characterization of selective metal complexing agents.

Herein we describe the synthesis and characterization of new sulfonated and carboxylated poly(propyleneimino) (PPI) dendrimers with the ethylenediamino (EDA) core, at generations 1, 2 and 3. By means of UV-Vis and EPR spectroscopy, using Cu(2+) as a probe, we concluded that these dendrimers show a specific pattern in the coordination of metal ions. In agreement with the UV-Vis studies, EPR spectra of carboxylated compounds are constituted by 3 different signals which appear and then disappear with increasing copper concentration, corresponding to the saturation of different copper complexation sites.

Spin probe analysis of microtubules structure and formation.

Microtubules (MTs) control cell replication, material transport and motion in eukaryotic cells, but MT role in several pathologies is still unknown. These functions are related to the MT physico-chemical properties and MT formation mode starting from tubulin molecules. This study describes a new method, based on the computer aided analysis of the electron paramagnetic resonance (EPR) spectra of selected spin probes to obtain structural and dynamical information on tubulins and MTs and the kinetics of MTs formation promoted by guanosine-5'-triphosphate (GTP).

Time evolution of the aggregation process of peptides involved in neurodegenerative diseases and preventing aggregation effect of phosphorus dendrimers studied by EPR.

A key pathological event of prion and Alzheimer diseases is the formation of prion and amyloid plaques generated by peptide aggregation in the form of fibrils. Dendrimers have revealed their ability to prevent fibril formation and therefore cure neurodegenerative diseases. To provide information about the kinetics and the mechanism of peptide fibril formation and about the ability of the dendrimers to prevent peptide aggregation, we performed a computer-aided EPR analysis of the selected nitroxide spin probe 4-octyl-dimethylammonium,2,2,6,6-tetramethyl-piperidine-1-oxyl bromide (CAT8) in water solutions of the β-amyloid peptide Aβ 1-28 and the prion peptide PrP 185-208, which contain the fibril nucleation sites, in the absence and in the presence of phosphorus dendrimers.