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PubMed1990

Superoxide anion radical induces lipid phase transitions that mimic temperature-induced phase-transition phenomenon of membrane lipids.

A biological membrane is shown to undergo lipid-phase transition leading to increased membrane fluidity when exposed to extraneously generated superoxide anion radical. This phase-transition is several folds higher in magnitude when compared to the temperature-induced fluidity change at the transition temperatures. This finding could have significant importance since an altered membrane configuration may involve aspects of biochemistry, biophysics or physiology.

Animals↗
PubMed2003

Itraconazole formulation studies of the melt-extrusion process with mixture design.

Itraconazole is a poorly water soluble compound. One method to increase the aqueous solubility of itraconazole is through formation of a solid dispersion. The purpose of this study is to develop a 40% w/w itraconazole formulation through solid dispersion formation, using hydroxypropyl-beta-cyclodextrin (HP-beta-CD) and hydroxypropylmethyl-cellulose (HPMC) as mixture components. The solid dispersion was obtained by melt-extrusion using a twin-screw corotating melt extruder. A D-optimal mixture design was applied for the development of the optimal itraconazole formulation. The itraconazole fraction varied between 20% w/w and 50% w/w in the mixture design and the HPMC and HP-beta-CD fractions varied between 10% w/w and 60% w/w. The itraconazole formulation was optimized by producing clear extrudates, minimizing the torque, and maximizing the glass transition temperature and the apparent itraconazole solubility in 0.1 N HCl. Regression models were developed for the torque, glass transition temperature, and apparent solubility of itraconazole. High itraconazole fraction in the mixture promoted a better melt processing (minimizes torque). High HPMC fraction (>33% w/w) resulted in clear extrudates, indicating a solid dispersion and resulted in high glass transition temperature of the melt. High HP-beta-CD fraction resulted in increased apparent itraconazole solubility in 0.1 N HCl. The optimal itraconazole formulation consisted of 45% w/w HPMC and 15% HP-beta-CD w/w.

2-Hydroxypropyl-beta-cyclodextrin↗
PubMed1988

Studies of interaction phenomena in aqueous-based film coatings containing soluble additives using thermal analysis techniques.

Interaction phenomena, in aqueous-based hydroxypropyl methylcellulose (HPMC) and polyvinyl alcohol (PVA) film-coating formulations containing water-soluble additives (citric acid and urea) have been examined by thermal methods to assess glass transition, softening, melting, plasticization, and crystallinity. The methods used were differential scanning calorimetry (DSC) and thermomechanical analysis (TMA) in penetration and expansion modes. In addition to the established thermal transitions occurring in HPMC and PVA at relatively high temperatures, transitions were also observed between 26 and 43 degrees C using TMA. These low temperature transitions, unlike those occurring at the higher temperatures, were low energy transitions and not influenced by the type and concentration of the additives incorporated. The results also showed that the plasticizing activities of citric acid and urea were as high as those of some currently used plasticizers. On a weight basis, urea was superior to citric acid as a plasticizer for either HPMC or PVA, but when their molar contents were considered, the position was reversed. Also, PVA crystallinity was depressed in the presence of the additives.

Calorimetry, Differential Scanning↗
PubMed1978

The effect of gramicidin A on the temperature dependence of water permeation through liposomal membranes prepared from phosphatidylcholines with different chains lengths.

The permeation of water through liposomal membranes composed of various saturated phosphatidylcholine plus gramicidin A was studied as a function of temperature. 1. The presence of gramicidin in the liposomal bilayers caused an increase in water permeability. Below the phase transition temperature this effect could be measured quite clearly in all the systems we tested, but the extent of the increase was largely dependent on the length of the hydrocarbon chains. 2. Increasing amounts of gramicidin caused a gradual disappearance of the abrupt change in the rate of water permeation near the gel-liquid crystalline phase transition temperature of dipalmitoyl phosphatidylcholine liposomes. Differential scanning calorimetry analysis of the system containing these relatively small amounts of gramicidin still showed a clear transition from the liquid crystalline to the gel state with only a slight reduction in the enthalpy change. 3. In liposomes composed of dimyristoyl, dipalmitoyl and saturated egg phosphatidylcholine there was a concomitant decrease in the activation energy of water permeation in the presence of gramicidin below and above the phase transition temperature. The activation energy for water permeation through longer chained distearoyl phosphatidylcholine liposomal bilayers was the same with or without gramicidin in the bilayer. 4. It is concluded that the ability of gramicidin to form conducting channels in a gel state bilayer depends on the thickness of the paraffin core.

Biological Transport↗
PubMed1995

Influence of monoglucosyldiacylglycerol and monoacylmonoglucosyldiacylglycerol on the lipid bilayer of the membrane from Acholeplasma laidlawii strain A-EF22.

The ability for 1,2-diacyl-3-O-(alpha-D-glucopyranosyl)-sn-glycerol (MGlcDAG) and 1,2-diacyl-3-O-(6-O-acyl-(alpha-D-glucopyranosyl))-sn-glycerol (MAMGlcDAG) to induce non-lamellar phases in a lipid mixture with an in vivo composition, prepared from Acholeplasma laidlawii membranes, has been investigated. The phase transition temperatures from lamellar to non-lamellar structures were studied with varying fractions of MGlcDAG and MAMGlcDAG. The transition temperature decreased from 73 +/- 2 degrees C for 20 mol% MGlcDAG to 43 +/- 1 degree C for 63 mol% MGlcDAG, in lipid mixtures where the other lipids are the native bilayer-forming lipids. MAMGlcDAG behaved differently and the phase transition temperatures were found to be almost constant and between 51-53 degrees C as the fraction of MAMGlcDAG varied between 11-45 mol%. It was also found that MAMGlcDAG can only be solubilized in low concentrations in the lipid bilayer, which is in good agreement with the fractions of MAMGlcDAG found in the membrane of A. laidlawii. Higher concentrations of MAMGlcDAG resulted in phase separations of lamellar liquid crystalline and gel/crystalline phases. It is concluded that MAMGlcDAG is far more capable than MGlcDAG to induce non-lamellar structures at lower concentrations. The results are discussed in terms of the model of lipid regulation previously proposed by this laboratory (Lindblom, G., Hauksson, J.B., Rilfors, L., Bergenståhl, B., Wieslander, A. and Eriksson, P.O. (1993) J. Biol. Chem. 268, 16198-16207), and the importance for the bilayer stability in cell membranes. It is proposed that the phase behaviour of the membrane lipids has far-reaching consequences for membrane function.

Acholeplasma laidlawii↗
PubMed1988

Study of pH- and temperature-induced transitions in F-protein (phosphofructokinase) by spectroscopy and microcalorimetry methods.

The temperature- and pH-induced transitions in F-protein (phosphofructokinase (ATP:D-fructose-6-phosphate 1-phosphotransferase, EC 2.7.1.11] have been studied by means of microcalorimetry and fluorescence and CD spectroscopy. An increase in pH from approx. 6.0 to approx. 8.0 causes a change in the protein state which seems to correspond to a shift of the dimer-tetramer equilibrium in favour of the tetramers. In the absence of phosphate, stability of the protein to temperature- and urea-induced denaturation at pH 6.0 is higher than that at pH 8.0. An addition of 150 mM phosphate results in a pronounced increase in the protein's stability in such a way that the protein becomes more stable at pH 8.0 than at pH 6.0. The shift of the denaturational heat capacity peak induced by the phosphate binding exceeds 25 degrees C at pH 8.0 and 9 degrees C at pH 6.0.

Animals↗
PubMed1989

Residual stress in several ceramometal systems.

Residual stress caused by a mismatch of alloy-porcelain thermal contraction can contribute to clinical failure of a ceramometal restoration. This investigation assessed thermal compatibility of three ceramometal alloys and two opaque porcelains. Thermal expansions of the alloys and porcelains were measured by using a straight push-rod dilatometer. Porcelain glass transition temperatures and expansion values were derived from length-versus-temperature curves. Residual stress states in alloy-porcelain pairs were assessed by comparing expansion values of the components at the porcelain glass transition temperatures. Above that temperature the porcelain viscosity is low and stress relief is possible, whereas below the glass transition the porcelain acts as a stress-supporting solid. Expansion values were in general agreement and glass transition temperatures were slightly lower than values previously reported for similar materials. Alloy-porcelain thermal compatibility for the materials tested appeared more dependent on the opaque porcelain than the alloy.

Chemical Phenomena↗
PubMed1980

Effects of gaseous anaesthetics and inert gases on the phase transition in smectic mesophases of dipalmitoyl phosphatidylcholine.

The phase transition in smectic mesophase of dipalmitoyl phosphatidyl-choline was studied under high pressures of helium (340 atm), nitrogen (340 atm), nitrous oxide (43 atm), cyclopropane (4.4 atm) and n-propane (8.2 atm), using a turbidimetric technique. Helium and nitrogen increased the transition temperature by 0.021 and 0.006 degree C/atm, respectively, compared with 0.024 degrees C/atm for hydrostatic pressure. Nitrous oxide reduced the transition by 0.58 degree C/atm. The hydrocarbon gases spread the transition width and lowered the transition temperature with increasing effect at higher doses. Comparisons with other membrane probes are made and the concentration of gases in the bilayer which lower the transition temperature by 1 degree C are estimated, in mol%: He, 10.2; N2, 13.2: N2O, 9.04; n-C3H8, 6.3 and cyclopropane, 12.8.

Anesthetics↗
PubMed1979

The influence of dioxan on the bilayer and monolayer phase transition of phospholipids.

The influence of 1.4.-dioxan on the bilayer phase transition of various phospholipids was studied by differential scanning calorimetry and turbidity measurements. The addition of 1.4.-dioxan to lipid bilayers decreases the transition temperature T(m) increases the transition enthalpy of the transition. The cooperativity of the transition is unaffected. The phospholipid monolayer transition from the liquid-condensed to the liquid-expanded phase was measured by recording area versus temperature curves at constant surface pressure (isobars). The monolayer transition temperature at constant surface pressure is increased when 1.4.-dioxan is added to the subphase. The change in molecular area becomes larger. A comparison of monolayer isobars on water and water/dioxan as subphase at constant surface tension rather than surface pressure leads to a decrease of the transition temperature on water/dioxan as subphase. This decrease as well as the larger change in molecular area at the monolayer transition can be correlated to the decrease in Tm and the increase in the transition enthalpy of the corresponding bilayer system. 1.4.-Dioxan seems to accumulate at the lipid head group/water interface, thus lowering the tension of the bilayer membrane. This cyclic ether can be used for altering the characteristics of bilayer membranes without disturbing the lipid chain organization.

Journal Article↗
PubMed1989

Temperature-absorption transition spectroscopy: a technique for estimating the relative charge densities on thiolated phosphate groups in nucleic acid analogues.

Various polynucleotides with well-defined sequences at low salt concentration have been studied using temperature-absorbtion transition spectroscopy to understand their conformations. It has been observed that the adopted technique can fairly estimate the relative charge densities at the thiolated phosphate groups in nucleic acid analogues at low salt concentrations.

Nucleic Acid Conformation↗
PubMed1975

Interaction of D-beta-hydroxybutyrate apodehydrogenase with phospholipids.

The interaction of a soluble homogeneous preparation of D-beta-hydroxybutyrate apodehydrogenase with phospholipid was studied in terms of restoration of enzymic activity and complex formation. The purified apoenzyme, which is devoid of lipid, is inactive. It is reactivated specifically by the addition of lecithin or mixtures of phospholipids containing lecithin. Mitochondrial phospholipid, i.e. the mixture of phospholipids in mitochondria, reactivates with the highest specific activity (approximately 100 micromol of DPN reduced/min/mg at 37 degrees and with the greatest efficiency (2.5 to 4 mol of lecithin/mol of enzyme subunit). Each of the lecithins of varying chain length and unsaturation reactivated the enzyme, albeit to differing extents and efficiencies. In general, lecithins containing unsaturated fatty acid moieties reactivated better than those containing the comparable saturated lipid. Optimal reactivation can be obtained for the various lecithins when they are microdispersed together with phosphatidylethanolamine. When the lecithins are added microdispersed together with both phosphatidylethanolamine and cardiolipin, maximal efficiency is obtained. Also, PC6:0 and 8:0 reactivate as soluble molecules, so that a phospholipid bilayer is not necessary to reactivate the enzyme. Complex formation was studied using gel exclusion chromatography. It can be shown that each of the phospholipids which reactivate combines with the apoenzyme. Mitochondrial phospholipid, which reactivates the best, binds most effectively; PC8:0, which reactivates with poor efficiency, can be shown to bind with low affinity, and negligible binding occurs at concentrations which do not reactivate the enzyme. Since the apoenzyme is apparently homogeneous and devoid of phospholipid or detergents, it would appear that reactivation does not involve reversal of inhibition such as by removal of a regulatory subunit or detergent from the catalytic subunit. Rather, we conclude that phospholipid is a necessary and integral portion of this enzyme whose active form is a phospholipid-protein complex. The apoenzyme also forms a complex with phosphatidylethanolamine and/or cardiolipin, which do not reactivate enzymic activity. Salt dissociates such complexes in contrast with the lecithin-apoenzyme complex. Binding of phospholipid is a necessary but not sufficient requisite for enzymic activity. The same energies of activation are obtained from Arrhenius plots for the membrane-bound enzyme and for the purified soluble enzyme reactivated with mitochondrial phospholipid or different lecithins. This observation is compatible with the view that the purified enzyme has not been adversely modified in the isolation. Furthermore, essentially the same energies of activation were obtained for saturated lecithins below their transition temperatures and for unsaturated lecithins above their transition temperatures. Hence, there is no indication that a lipid phase transition occurs to influence the activity of this enzyme.

Animals↗
PubMed1988

Effects of sugar alcohols and disaccharides in inducing the hexagonal phase and altering membrane properties: implications for diabetes mellitus.

A number of sugars lowered the bilayer to hexagonal phase transition temperature of dielaidoylphosphatidylethanolamine. Disaccharides had the greatest effect followed by sugar alcohols. The monosaccharides, glucose and galactose had no effect on this phase transition temperature. The sugars promoted vesicle leakage only under conditions where the lipid was near its hexagonal phase transition temperature. Leakage from lipids in the bilayer state was inhibited by the sugars. Polyols, such as sorbitol, promote hexagonal phase formation and alter membrane permeability. These membrane effects may contribute to the damage caused by sorbitol accumulation in certain tissues of diabetic patients.

Calorimetry, Differential Scanning↗
PubMed1993

The influence of thermal treatment on the physical-mechanical and dissolution properties of tablets containing poly(DL-lactic acid).

Five molecular weight grades of poly(DL-lactic acid) (PLA) were incorporated as organic and aqueous pseudolatex binders into matrix tablet formulations containing microcrystalline cellulose and the model drug theophylline. The tablets were thermally treated to temperatures above and below the glass transition temperature (Tg) of the PLA. The results of the dissolution studies showed that thermally treating the tablets to temperatures above the Tg of the PLA significantly retarded the matrix drug release compared to tablets which were not thermally treated. The retardation in drug release could be attributed to a stronger compact and a more efficient redistribution of polymer throughout the tablet matrix, based on fundamental principles of annealing. In addition, results from tablet index testing supported the dissolution results. The bonding index of the compact formulations increased after thermal treatment above the Tg of the PLA. Gel permeation chromatography and differential scanning calorimetry studies demonstrated that thermal treatment had no significant effect on the molecular weight and the glass transition temperature of (PLA) alone and in combination with other components of the tablet formulation.

Calorimetry, Differential Scanning↗
PubMed2003

influence of the molecular structures on the high-pressure and low-temperature phase transitions of plastic crystals.

The crystal structures of tert-butyl-tris(trimethylsilyl)silane, Si[C(CH(3))(3)](1)[Si(CH(3))(3)](3) (Bu1), and di-tert-butyl-bis(trimethylsilyl)silane, Si[C(CH(3))(3)](2)[Si(CH(3))(3)](2) (Bu2), at room temperature and at 105 K have been determined by X-ray powder diffraction; the high-pressure behavior for pressures between 0 and 5 GPa is reported. The room-temperature structures have cubic Fm3m symmetry (Z = 4) with a = 13.2645 (2) A, V = 2333.87 (4) A(3) for Bu1 and a = 12.9673 (1) A, V = 2180.46 (3) A(3) for Bu2. The molecules are arranged in a cubic close packing (c.c.p.) and exhibit at least 48-fold orientational disorder. Upon cooling both compounds undergo a first-order phase transition at temperatures T(c) = 230 (5) K (Bu1) and T(c) = 250 (5) K (Bu2) into monoclinic structures with space group P2(1)/n. The structures at 105 K have a = 17.317 (1), b = 15.598 (1), c = 16.385 (1) A, gamma = 109.477 (4) degrees, V = 4172.7 (8) A(3) and Z = 8 for Bu1and a = 17.0089 (9), b = 15.3159 (8), c = 15.9325 (8) A, gamma = 110.343 (3) degrees, V = 3891.7 (5) A(3) and Z = 8 for Bu2. The severe disorder of the room-temperature phase is significantly decreased and only a two- or threefold rotational disorder of the molecules remains at 105 K. First-order phase transitions have been observed at pressures of 0.13-0.28 GPa for Bu1 and 0.20-0.24 GPa for Bu2. The high-pressure structures are isostructural to the low-temperature structures. The pressure dependencies of the unit-cell Volumes were fitted with Vinet equations of state and the bulk moduli were obtained. At still higher pressures further anomalies in the pressure dependencies of the lattice parameters were observed. These anomalies are explained as additional disorder-order phase transitions.

Journal Article↗
PubMedDate not supplied

Haemolytic properties of cereal 5-n-alk(en)ylresorcinols.

The haemolytic activity of 5-n-alk(en)ylresorcinols is temperature dependent and correlated to their transition temperatures. The values of the parameters describing the 5-n-alk(en)ylresorcinol-induced red blood cell lysis indicate strong affinity of the compounds to the membrane and their high lytic capacity. The affinity of the compounds for the membrane decrease with the increasing quantity of the molecules incorporated into the erythrocyte membrane and is much higher for saturated resorcinols than unsaturated ones. The amount of 5-n-alk(en)ylresorcinol molecules bound to the membrane at a hundred percent lysis is about eighty times and eleven times (for alkyl and alkenyl derivatives respectively) higher than at zero percent lysis. Estimated free energy of erythrocyte lysis was similar for alkyl and alkenyl derivatives of resorcinol provided the preparation of the resorcinolic suspensions above their transition temperatures.

Edible Grain↗
PubMed1979

Thermal characterization of citric acid solid dispersions with benzoic acid and phenobarbital.

The glass transition temperatures of citric temperatures of citric acid glass were determined by differential scanning calorimetry to be 10.2 and 13.5 degrees for in situ and bulk-prepared samples, respectively. Mechanical stress on citric acid glass induced foci for crystallization. Benzoic acid addition to citric acid glass decreased its glass transition temperature while phenobarbital addition increased its glass transition temperature, the latter forming a glass solution.

Benzoates↗
PubMed1980

Phase transitions of alkyl ether analogs of phosphatidylcholine.

The phase-transition temperatures of aqueous dispersions of diester, monoether and diether analogs of phosphatidylcholine were determinmed using transparinaric acid as a fluorescent probe. The diether analog of phosphatidylcholine has a higher phase-transition temperature, whilst the monoether analog has a lower phase-transition temperature than their diester counterpart.

Liposomes↗
PubMed1983

Phenobarbital modulates the (Na+, K+)-stimulated ATPase and Ca2+-stimulated ATPase activities by increasing the bilayer fluidity of dog brain synaptosomal plasma membranes.

The binding of [14C]phenobarbital into synaptosomal plasma membranes of dog brain follows a sigmoid path. The "best fit" curve of this binding is the one described by the Hill equation (r2 less than 0.93 and Hill coefficient, n = 1.32). (Na+, K+)-stimulated ATPase and Ca2+-stimulated ATPase activities are modulated by phenobarbital. Arrhenius plots of (Na+, K+, Mg2+)-dependent ATPase revealed that phenobarbital (2 mM) lowered the transition temperature and altered the Arrhenius activation energies of this enzyme. The allosteric inhibition by F- of the (Na+, K+)-stimulated ATPase was studied in control and phenobarbital-treated membranes. The lowering of the transition temperature and changes in Arrhenius activation energy about the transition temperature in combination with changes observed in the allosteric properties of the (Na+, K+)-stimulated ATPase by F-, produced by phenobarbital, would be expected if it is assumed that phenobarbital "fluidizes" synaptosomal plasma membranes.

Animals↗