Interaction Of Oleic Acid Research Articles

Interactions of Cellulase and Oleic Acid Solution Mixtures

AbstractThe interaction of oleic acid, as an anionic detergent, with cellulase has been investigated using different techniques (surface tension, turbidity and FTIR). The surface tension measurements show that the CMC of the oleic acid-cellulase mixture is lower than that of the individual components. The interaction in this case is defined as attractive and the mixture exhibits synergism. Also, it is found that the area per molecule for the oleic acid/cellulase mixed isotherm is lower than area of the pure oleic acid. This decrease in the area/molecule is due to the arrangement of cellulase molecules in-between the oleic acid chains. Turbidity measurements indicate the formation of two complexes. Complex 1 is obtained at low oleic concentrations (< 10−4 M) with compact size giving a high turbidity. Complex 2 is formed at higher oleic concentrations (> 10−4 M) where the formed aggregates were precipitated and the turbidity was decreased. The changes in the FTIR spectrum features of cellulase after oleic acid addition indicate an interaction between cellulase and oleic acid in their mixture.

Phase Equilibria in Triacylglycerols – Ethanol – Oleic Acid – Athyl Oleate Quasi-Quaternary System

<p>In order to use waste vegetable oils to produce biodiesel a possibility of reagents (sunflower oil and ethanol) mixture homogenization under the simultaneous effect of two cosolvents (oleic acid and ethyl oleate) was investigated. The possibility of action of oleic acid and ethyl oleate as cosolvents was analyzed with GSP model. For qualitative assessment of the intermolecular interaction parameter ξ was used. This parameter is a measure <br />of the ratio between cross-association (solvation) energy A–B and self-association (association) energies A–A and B–B. It was shown that most important role at intermolecular interactions of oleic acid and ethyl oleate with triglycerides belonged to dispersion forces. Predominant contribution of hydrogen bonds in the interaction of oleic acid and ethyl oleate with ethanol was shown. The prediction of improving the effect of the cosolvents with temperature increasing was done, and it was confirmed by experimental results.<br />The effect of oleic acid and ethyl oleate as cosolvents for homogenization of mixtures of sunflower oil and ethanol was investigated experimentally by studying the phase equilibria in the quasi-quaternary system triacylglycerols (sunflower oil) –ethanol –oleic acid –ethyl oleate at 30, 40, 50, 60 and 70 °C. The results of the experiments are presented in the form of phase diagrams of quasi-ternary boundary systems: triacylglycerols –oleic acid –ethanol and triacylglycerols –ethyl oleate –ethanol, and the phase <br />diagrams of composition tetrahedron sections with five different ratios of components oleic acid: ethyl oleate. Generalization of the research results is presented in the form of polythermal phase diagram for the system triacylglycerols –ethanol –oleic acid –ethyl oleate. Solubility polytherms (from 30 to 70 °C) for the system triacylglycerols –ethanol –mixed cosolvent with different ratios of oleic acid and ethyl oleate were plotted.</p>

Interaction of Oleic Acid with Dipalmitoylphosphatidylcholine (DPPC) Bilayers Simulated by Molecular Dynamics

The fatty acid oleic acid (OA) is known to modulate the structure of membranes, which forms the basis for a number of its important applications including its use as a therapeutic supplement to reduce the risk of cardiovascular disease, in molecule delivery systems such as liposomes, and as a skin permeability enhancer. While a number of studies have investigated the effect of OA on lipid membranes, our understanding of its mechanisms of action at the molecular level remains rudimentary. We have carried out molecular dynamics simulations using coarse-grained models to investigate the interactions of OA at a range of concentrations with a dipalmitoylphosphatidylcholine (DPPC) bilayer in the liquid-crystalline phase. We have also investigated the relative permeability of the bilayers to model hydrophilic and hydrophobic penetrants by means of chemical potential calculations. The results indicate that OA is able to disperse homogeneously into the bilayer at all concentrations without much perturbation. OA appears to slightly weaken the lateral forces between lipid headgroups, and as the concentration of OA increases this manifests itself as a slight decrease in the area compressibility modulus and a minor increase in the diffusion rate of the OA molecules. While the chemical potential profiles showed little or no variation as a function of OA concentration, the frequency of water permeation events was found to double, indicating some OA-induced permeability enhancement. The study suggests that physiological effects of OA are probably more subtle rather than via gross perturbation of the structure, or that its significant effects are restricted to more condensed membrane structures such as the gel phase.

Interactions of oleic acid and model stratum corneum membranes as seen by 2H NMR

We have investigated the mechanism through which the penetration enhancer oleic acid acts on stratum corneum (SC) model membranes (bovine brain ceramide:cholesterol:palmitic acid, 1:1:1 molar ratio). We used solid state deuterium nuclear magnetic resonance to monitor such multilamellar SC dispersions containing either cholesterol-d 6, palmitic acid-d 31, or oleic acid-d 2 as a function of both fatty acid concentration (2:2:1:1 and 1:1:1:1 bovine brain ceramide:cholesterol:palmitic acid:oleic acid) and temperature (18–75 °C). Our results show that below 40 °C, oleic acid (OA) is in an ‘isotropic’ phase, indicating that it has not incorporated into the lamellar membrane phase. At and above the SC model membrane's crystalline to liquid crystalline melting temperature, T m = 40–42 °C, OA interacts with lamellar SC membranes with a slight dependence on OA concentration. T m does not change upon the exposure of the SC model membrane to OA, nor do we see any significant change in membrane chain disorder as monitored by the labelled PA. However, the spectra of both the palmitic acid (PA) and cholesterol SC model membrane components contain an isotropic peak that grows with increasing temperature. Our results thus indicate that oleic acid extracts a fraction of the endogenous SC membrane components, promoting phase separation in the SC membrane system. Reducing the proportion of crystalline lipids and creating more permeable OA-rich domains is a plausible mechanism that explains how OA enhances transdermal penetration.

Adsorption of Oleic Acid at Sillimanite/Water Interface

The interaction of oleic acid at sillimanite–water interface was studied by adsorption, FT-IR, and zeta potential measurements. The isoelectric point (IEP) of sillimanite obtained at pH 8.0 was found to shift in the presence of oleic acid. This shift in IEP was attributed to chemisorption of oleic acid on sillimanite. Adsorption experiments were conducted at pH 8.0, where the sillimanite surface is neutral. The adsorption isotherm exhibited a plateau around 5 μmol/m2 that correspond to a monolayer formation. Adsorption of oleic acid on sillimanite, alumina, and aluminum hydroxide was studied by FT-IR. Chemisorption of oleic acid on the above substrates was confirmed by FT-IR studies. Hydroxylation of mineral surface was found to be essential for the adsorption of oleic acid molecules. These surface hydroxyl sites were observed to facilitate deprotonation of oleic acid and its subsequent adsorption. Thus protons from oleic acid react with surface hydroxyl groups and form water molecules. Based on the experimental results, the mechanism of oleic acid adsorption on mineral substrate was proposed. Free energy of adsorption was estimated using the Stern–Graham equation for a sillimanite–oleate system.

Stimulation of plasmin activity by oleic acid.

The amidolytic activity of plasmin with the chromogenic substrate H-D-valyl-L-leucyl-L-lysine p-nitroanilide (S-2251) is stimulated by oleic acid in a dose-dependent and saturable fashion. The activity of plasmin on S-2251 in the presence of oleic acid followed a sigmoidal kinetic pattern, with an almost 4-fold stimulation of activity at 60 microM-oleic acid. Half-maximal stimulation occurred at an oleic acid level of 19.5 microM. The amino acid analogue 6-aminohexanoic acid (AHA), which is known to bind to lysine-binding sites in plasmin, suppressed the stimulatory effect of oleic acid in a concentration-dependent manner; at 0.3 mM-AHA, about 70% of the oleic acid-dependent enhancement of plasmin activity was abolished. The l/v versus 1/[S] plot for plasmin changed in the presence of oleic acid from a linear to a non-linear curve, suggesting positive co-operativity. 14C-labelled oleic acid bound to plasmin, and the bound ligand was displaced by an excess of unlabelled oleic acid. Oleic acid also produced a marked (40-fold) stimulation of the plasminogen-dependent cleavage of S-2251 by urokinase. A half-maximal effect on plasminogen activation was obtained at 40 microM-oleic acid. The present findings suggest that the ability of oleic acid to stimulate plasmin activity and to enhance the conversion of plasminogen to plasmin depends on the interaction of oleic acid with specific lysine-binding sites in plasmin.

Inhibitors directed to binding domains in neutrophil elastase

Human neutrophil elastase (HNE) can be inhibited by unsaturated fatty acids, including oleic acid [Ashe, B. M., & Zimmerman, M. (1977) Biochem. Biophys. Res. Commun. 75, 194-199; Cook, L., & Ternai, B. (1988) Biol. Chem. Hoppe-Seyler 369, 627-631], but is not affected by saturated fatty acids. We have shown that the interaction of oleic acid with HNE can be characterized by two apparent inhibitory modes: a high-affinity mode (Ki = 48 +/- 3 nM), resulting in partial noncompetitive inhibition (87% residual activity), and a competitive inhibitory mode of lower affinity (Ki = 16 +/- 1 microM). Binding of oleate in the high-affinity mode induces a blue shift in the endogenous fluorescence arising from the tryptophan residues in HNE. This shift is maximal in the presence of 1 microM oleate; higher concentrations of fatty acid have no further effect on the fluorescence spectrum. The negatively charged fluorescent ester of oleic acid and hydroxypyrenetrisulfonate (HPTSoleate) interacts with HNE at an apparent single site (Ki = 44 +/- 3 nM), resulting in competitive inhibition. A blue shift in the emission maximum of the pyrene fluorescence at 410 nm and a decrease in the ratio of the intensities of the maximum at 388 and 410 nm indicate that upon binding to HNE the environment of the pyrene ring in HPTSoleate becomes more hydrophobic.(ABSTRACT TRUNCATED AT 250 WORDS)

Interactions of oleic acid with liver fatty acid binding protein: a carbon-13 NMR study [Erratum to document cited in CA108(7):51580v

Interactions of oleic acid with liver fatty acid binding protein: a carbon-13 NMR study [Erratum to document cited in CA108(7):51580v

Interactions of oleic acid with liver fatty acid binding protein: a carbon-13 NMR study.

13C NMR spectroscopy was used to probe the structural interactions between carboxyl-13C-enriched oleic acid (18:1) and rat liver fatty acid binding protein (FABP) and the partitioning of 18:1 between FABP and unilamellar phosphatidylcholine (PC) vesicles. Spectra of systems containing 2-8 mol of 18:1/mol of FABP (but no PC) exhibited one carboxyl resonance (182.2 ppm) corresponding to FABP-bound 18:1. At pH values less than 8.0, an additional carboxyl resonance, corresponding to unbound 18:1 in a lamellar phase, was observed. Both resonances exhibited ionization shifts with estimated apparent pKa values of less than 5 (bound 18:1) and greater than 7 (unbound 18:1). The intensity of the resonance corresponding to FABP-bound 18:1 increased with increasing 18:1/FABP mole ratio and at 8/1 mole ratio indicated that at least 2 and 6 mol of 18:1/mol of FABP were FABP-bound at pH 7.4 and 8.6, respectively. NMR spectra of systems containing equal concentrations (w/v) of FABP and PC and from 1 to 4 mol of total fatty acid (FA)/mol of FABP exhibited two 18:1 carboxyl resonances (182.2 and 178.5 ppm, pH 7.4). The downfield resonance corresponded to FABP-bound 18:1 and the upfield resonance to PC vesicle bound 18:1. At 1/1 mole ratio (FA/FABP), the intensities of both resonances were approximately equal, but at 4/1 mole ratio the resonance for PC vesicle bound 18:1 was 3-fold more intense than that for FABP-bound 18:1. The following conclusions are reached: (i) The carboxyl groups of 18:1 bound to liver FABP experience only one type of binding environment (the aqueous milieu adjacent to the protein surface).(ABSTRACT TRUNCATED AT 250 WORDS)

The mechanism of fatty acid adsorption in the presence of fluorite, calcite and barite

The interaction of oleic acid with fluorite, calcite and barite has been studied using solubility, oleate abstraction, electrophoretic mobility and Hallimond-tube flotation measurements. Abstraction of oleate from aqueous solution corresponds to the precipitation of the metal oleate. Multilayers of metal oleate inhibits the dissolution of the minerals and prevents true equilibrium from being obtained. Flotation is not only dependent on the amount of oleate abstracted but also on the strength of adhesion of the precipitated metal oleate to the minerals. Selectivity between the flotation of calcite, fluorite and barite is unlikely to be obtained by varying the pH because similar responses are observed.