Non-linear van't Hoff behavior in pulmonary surfactant model membranes.

Pulmonary surfactant exhibits phase coexistence over a wide range of surface pressure and temperature. Less is known about the effect of temperature on pulmonary surfactant models. Given the lack of studies on this issue, we used electron paramagnetic resonance (EPR) and nonlinear least-squares (NLLS) simulations to investigate the thermotropic phase behavior of the matrix that mimics the pulmonary surfactant lipid complex, i.e., the lipid mixture composed of dipalmitoyl phosphatidylcholine (DPPC), palmitoyl-oleoyl phosphatidylcholine (POPC) and palmitoyl-oleoyl phosphatidylglycerol (POPG). Irrespective of pH, the EPR spectra recorded from 5°C to 25°C in the DPPC/POPC/POPG (4:3:1) model membrane contain two spectral components corresponding to lipids in gel-like and fluid-like phases, indicating a coexistence of two domains in that range. The temperature dependence of the distribution of spin labels between the domains yielded nonlinear van't Hoff plots. The thermodynamic parameters evaluated were markedly different for DPPC and for the ternary DPPC/POPC/POPG (4:3:1) membranes and exhibited a dependence on chemical environment. While enthalpy and entropy changes for DPPC were always positive and presented a quadratic behavior with temperature, those of the ternary mixture were linearly dependent on temperature and changed from negative to positive values. Despite that, enthalpy-entropy compensation takes place in the two systems. The thermotropic process associated with the coexistence of the two domains is entropically-driven in DPPC and either entropically- or enthalpically-driven in the pulmonary surfactant membrane depending on the pH, ionic strength and temperature. The significance of these results to the structure and function of the pulmonary surfactant lipid matrix is discussed.

Ferromagnetic resonance for the quantification of superparamagnetic iron oxide nanoparticles in biological materials.

The aim of the present work is the presentation of a quantification methodology for the control of the amount of superparamagnetic iron oxide nanoparticles (SPIONs) administered in biological materials by means of the ferromagnetic resonance technique (FMR) applied to studies both in vivo and in vitro. The in vivo study consisted in the analysis of the elimination and biodistribution kinetics of SPIONs after intravenous administration in Wistar rats. The results were corroborated by X-ray fluorescence. For the in vitro study, a quantitative analysis of the concentration of SPIONs bound to the specific AC133 monoclonal antibodies was carried out in order to detect the expression of the antigenic epitopes (CD133) in stem cells from human umbilical cord blood. In both studies FMR has proven to be an efficient technique for the SPIONs quantification per volume unit (in vivo) or per labeled cell (in vitro).

Ferromagnetic resonance for the quantification of superparamagnetic iron oxide nanoparticles in biological materials

The aim of the present work is the presentation of a quantification methodology for the control of the amount of superparamagnetic iron oxide nanoparticles (SPIONs) administeredin biological materials by means of the ferromagnetic resonance technique (FMR) applied to studies both in vivo and in vitro. The in vivo study consisted in the analysis of the eliminationand biodistribution kinetics of SPIONs after intravenous administration in Wistar rats. The results were corroborated by X-ray fluorescence. For the in vitro study, a quantitative analysisof the concentration of SPIONs bound to the specific AC133 monoclonal antibodies was carriedout in order to detect the expression of the antigenic epitopes (CD133) in stem cells from human umbilical cord blood. In both studies FMR has proven to be an efficient technique forthe SPIONs quantification per volume unit (in vivo) or per labeled cell (in vitro).

Weak exchange interaction supported by a biologically relevant long chemical bridge in a Cu-peptide model compound.

The copper complex of the dipeptide L-alanyl-L-phenylalanine, catena-(L-alaninate-L-phenylalaninate-copper(II) monohydrate), identified as Cu(II)Ala-Phe, provides a convenient system to study a weak exchange interaction between unpaired spins transmitted through a biologically relevant long chemical bridge (18.34 A). In this complex, the copper ions are arranged in two symmetry-related anisotropic layers parallel to the ab plane at 13.17 A, separated by a double layer of water molecules. The equatorial-equatorial bridge considered as the most relevant path for exchange interactions between copper ions in neighbor layers contains 11 diamagnetic atoms (including three hydrogens), with two covalent amidate bridges plus three weak and moderate H bonds that go across the water layer. This interaction was studied using electron paramagnetic resonance in single-crystal samples, at 9.5 and 34.5 GHz. The measured magnitude of the interlayer interaction, |J3|/kB = 1.7(2) x 10(-3) K, is discussed in terms of values obtained for similar paths in other model compounds and in proteins. These results in model systems provide information that may be important in understanding biological functions at the molecular level.