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PubMed2005

The Alzheimer beta-peptide shows temperature-dependent transitions between left-handed 3-helix, beta-strand and random coil secondary structures.

The temperature-induced structural transitions of the full length Alzheimer amyloid beta-peptide [A(beta)(1-40) peptide] and fragments of it were studied using CD and 1H NMR spectroscopy. The full length peptide undergoes an overall transition from a state with a prominent population of left-handed 3(1) (polyproline II; PII)-helix at 0 degrees C to a random coil state at 60 degrees C, with an average DeltaH of 6.8 +/- 1.4 kJ.mol(-1) per residue, obtained by fitting a Zimm-Bragg model to the CD data. The transition is noncooperative for the shortest N-terminal fragment A(beta)(1-9) and weakly cooperative for A(beta)(1-40) and the longer fragments. By analysing the temperature-dependent 3J(HNH(alpha)) couplings and hydrodynamic radii obtained by NMR for A(beta)(1-9) and A(beta)(12-28), we found that the structure transition includes more than two states. The N-terminal hydrophilic A(beta)(1-9) populates PII-like conformations at 0 degrees C, then when the temperature increases, conformations with dihedral angles moving towards beta-strand at 20 degrees C, and approaches random coil at 60 degrees C. The residues in the central hydrophobic (18-28) segment show varying behaviour, but there is a significant contribution of beta-strand-like conformations at all temperatures below 20 degrees C. The C-terminal (29-40) segment was not studied by NMR, but from CD difference spectra we concluded that it is mainly in a random coil conformation at all studied temperatures. These results on structural preferences and transitions of the segments in the monomeric form of A(beta) may be related to the processes leading to the aggregation and formation of fibrils in the Alzheimer plaques.

Alzheimer Disease↗
PubMed2002

Effect of crystallite size on the thermal phase change and porous properties of boehmite.

The effect of crystallite size on the thermal phase change and porous properties of boehmite was investigated using boehmites with crystallite sizes of 2.9 to 24.4 nm and boehmite gels prepared by precipitation and hydrothermal methods. The dehydroxylation temperature of boehmite increases, its phase transition temperature from gamma- to theta-Al(2)O(3) decreases and the theta- to alpha-Al(2)O(3) transition temperature increases as the crystallite size of the boehmite increases. Boehmite with a crystallite size of approximately 5 nm shows the highest specific surface area and greatest thermal stability. This boehmite contains pores of about 2-3 nm radius, suggested to be responsible for the superior porous properties and thermal stability.

Aluminum Hydroxide↗
PubMed1994

Relationship between the infectivity of influenza virus and the ability of its fusion peptide to perturb bilayers.

The amino terminal segment of the HA2 protein of influenza virus has been identified as an important region for membrane fusion. We demonstrate that there is an association between the ability of model peptides corresponding to this region of the HA2 protein to promote the formation of inverted phases and the fusogenicity of the intact virus. The wild type virus can fuse to membranes at pH 5 but not at pH 7.4. We show that the fusion peptide of the wild type virus lowers the bilayer to hexagonal phase transition temperature of dipalmitoleoylphosphatidylethanolamine at pH 5 but at pH 7.4 it raises this transition temperature. In addition it has been shown that site specific mutagenesis resulting in the substitution of Gly with Glu leads to a loss of viral infectivity. These same amino acid substitutions in the viral fusion peptide result in the peptide no longer being able to lower the bilayer to hexagonal phase transition temperature, even at acidic pH. The wild type fusion peptide promotes the formation of structures which give rise to isotropic 31P NMR spectra at pH 5.0 but not at pH 7.4. The two altered sequences of the fusion peptide, corresponding to the Glu to Gly mutations, do not promote isotropic 31P NMR signals at acidic pH. These results indicate that the fusogenicity of influenza virus is dependent, in part, on the ability of the amino terminal region of HA2 to disrupt stable bilayer packing and to induce curvature strain corresponding to inverted phase structures.

Amino Acid Sequence↗
PubMed2005

Distinct difference in ionic transport behavior in polymer electrolytes depending on the matrix polymers and incorporated salts.

Two different electrolyte salts, lithium bis(trifluoromethanesulfonyl)imide (LiTFSI), and a room temperature ionic liquid, 1-ethyl-3-methylimidazolium bis(trifluoromethanesulfonyl)imide (EMITFSI), were incorporated into network polymers to obtain ion-conductive polymer electrolytes. Network polymers of poly(ethylene oxide-co-propylene oxide) (P(EO/PO)) and poly(methyl methacrylate) (PMMA) were chosen as matrixes for LiTFSI and EMITFSI, respectively. Both of the polymer electrolytes were single-phase materials and were completely amorphous. Ionic conductivity of the polymer electrolytes was measured over a wide temperature range, with the lowest temperatures close to or below the glass transition temperatures (Tg). The Arrhenius plots of the conductivity for both of the systems exhibited positively curved profiles and could be well fit to the Vogel-Tamman-Fulcher (VTF) equation. The conductivity of the PMMA/EMITFSI electrolytes was higher at most by 3 orders of magnitude than that of the LiTFSI/P(EO/ PO) electrolytes at ambient temperature. When the ideal glass transition temperature, T0 (one of the VTF fitting parameters), was compared with the Tg, a difference in the ionic conduction was apparent in these systems. In the P(EO/PO)/LiTFSI electrolytes, the T0 and Tg increased in parallel with salt concentration and the T0 was lower than the Tg by ca. 50 degrees C. On the contrary, the difference between the T0 and the Tg increased with increasing content of PMMA in the PMMA/EMITFSI electrolytes, with the observed difference in the concentration range studied reaching up to ca. 100 degrees C. The conductivity at the Tg, sigma(Tg), for the LiTFSI/P(EO/PO) electrolytes was on the order of 10(-14-)10(-13) S cm(-1) and increased with increasing salt concentration, whereas that for the PMMA/EMITFSI polymer electrolytes reached 10(-7) S cm(-1) when the concentration of PMMA was high. The ion transport mechanism was discussed in terms of the concepts of coupling/decoupling and strong/fragile for the two different polymer electrolytes.

Journal Article↗
PubMed1977

Physical properties of isolated complexes of human and bovine A-I apolipoproteins with L-alpha-dimyristoyl phosphatidylcholine.

Human or bovine A-I apolipoproteins in solution form complexes with sonicated L-alpha-dimirystoyl phosphatidylcholine at 23 and 37 degrees, but not at 8 degrees, suggesting a strong dependence of the interaction on the physical state of the lipid (phase transition temperature 23 degrees). Complexes were isolated by gel filtration on a Sepharose 4B column and were subsequently analyzed for protein and lipid content, molecular weight, and physical state of the lipid portion. The average stoichiometry of all complexes, regardless of the initial concentrations or ratios of protein and lipid, was constant: 90 +/- 20 mol of phospholipid/mol of protein monomer, suggesting a highly cooperative interaction. Sedimentation equilibrium experiments indicated homogeneous macromolecular preparations and gave molecular weights around 235,000 (+/- 15%) for the complexes, with the human and bovine apo-A-I proteins contributing 77,000 (+/- 10%), i.e. about three protein subunits per complex. The lipid portion of the complexes retained some characteristics of a bilayer: it had a broad phase transition with a midpoint at 25.5 degrees as reported by the fluorescence polarization of the lipophilic probe diphenylhexatriene. Above the phase transition temperature the mobility of the phospholipids in the complexes with both apo-A-I proteins was considerably decreased relative to the pure L-alpha-dimyristoyl phosphatidylcholine dispersion; below the phase transition temperature the opposite was true, i.e. the protein fluidized the lipids. The results indicate that apol-A-I proteins interact stoichiometrically with L-alpha-dimyristoyl phosphatidylcholine vesicles above the gel to liquid-crystalline transition temperature of the lipid, promoting the destruction of vesicles and the formation of well defined particles of the general size of high density serum lipoproteins.

Animals↗
PubMed1977

Effect of lysolecithin on the structure and permeability of lecithin bilayer vesicles.

In order to elucidate the role of lysolecithin in membranes, we have examined the effect of lysolecithin on the structure and permeability of lecithin bilayer membranes. Small L-alpha-dimyristoyllecithin (DML) vesicles with myristoyllysolecithin (MLL) incorporated as well as small L-alpha-dipalmitoyllecithin (DPL) vesicles with palmitoyllysolecithin (PLL) were studied by nuclear magnetic resonance (NMR) methods at temperatures both above and below the alpha-gel in equilibrium liquid crystalline phase transition temperature (Tc) and as a function of the concentration of the incorporated lysolecithin. Europium (III) ion was used as a probe to measure the permeability of the vesicular bilayer membrane. At temperatures below Tc, these vesicles were found to be extremely permeable to europium (III) ions. The ion translocation was found to be too fast to be measured by the NMR method under these conditions. However, above the phase transition temperature the ionic permeability decreases to a rate which could be conveniently monitored, and the permeability was shown to increase with temperature and lysolecithin concentration. Analysis of the lysolecithin concentration dependence suggests the formation of ion channels within the lipid bilayer involving four lysolecithin molecules. The data below Tc suggest a phase separation below the phase transition temperature of the host lipid, leading to the formation of patches of lysolecithin molecules within the lecithin matrix. These lysolecithin clusters are presumably long-lived under these conditions and are sufficiently structurally perturbed or disordered to serve as channels for rapid ion permeation.

Kinetics↗
PubMed2003

Zero-sized effect of nano-particles and inverse homogeneous nucleation. Principles of freezing and antifreeze.

It was found that freezing of water in terms of homogeneous nucleation of ice never occurs even in ultra-clean micro-sized water droplets under normal conditions. More surprisingly, at sufficiently low supercoolings, foreign nano-particles exert no effect on the nucleation barrier of ice; it is as if they physically "vanished." This effect, called hereafter the "zero-sized" effect of foreign particles (or nucleators), leads to the entry of a so-called inverse homogeneous-like nucleation domain, in which nucleation is effectively suppressed. The freezing temperature of water corresponds to the transition temperature from the inverse homogeneous-like nucleation regime to foreign particle-mediated heterogeneous nucleation. The freezing temperature of water is mainly determined by (i) the surface roughness of nucleators at large supercoolings, (ii) the interaction and structural match between nucleating ice and the substrate, and (iii) the size of the effective surface of nucleators at low supercoolings. Our experiments showed that the temperature of -40 degrees C, commonly regarded as the temperature of homogeneous nucleation-mediated freezing, is actually the transition temperature from the inverse homogeneous-like nucleation regime to foreign particle-mediated heterogeneous nucleation in ultra-clean water. Taking advantage of inverse homogeneous-like nucleation, the interfacial tensions between water and ice in very pure water and antifreeze aqueous solutions were measured at a very high precision for the first time. The principles of freezing promotion and antifreeze and the selection for the biological ice nucleation and antifreeze proteins are obtained. The results provide completely new insights into freezing and antifreeze phenomena and bear generic implications for all crystallization systems.

Antifreeze Proteins↗
PubMed1998

Interactions of cyclodextrins with DPPC liposomes. Differential scanning calorimetry studies.

The interaction of cyclodextrins (CDs) with dipalmitoylphosphatidylcholine (DPPC) liposomes has been studied using differential scanning calorimetry (DSC). The phase transition temperature and the enthalpy change due to the gel-to-liquid crystalline phase transition of the liposomes were measured in the presence of alpha-CD, beta-CD, gamma-CD, heptakis (2,6-di-O-methyl)-beta-CD (DOM-beta-CD), heptakis (2,3,6-tri-O-methyl)-beta-CD (TOM-beta-CD) and 2-hydroxylpropyl beta-CD, respectively. The effects on the change of enthalpy of the transition temperature were remarkable in the order of DOM-beta-CD > alpha-CD > TOM-beta-CD. The residual CDs caused scarcely detectable changes in the enthalpy changes and the transition temperatures. In order to clarify the DSC curves in the presence of the CDs mentioned above, the type of interactions which occurred between CDs and DPPC liposomes were studied. Consequently, it was found that DOM-beta-CD forms a soluble complex and alpha-CD forms an insoluble complex with DPPC liposomes, whereas only a slight amount of TOM-beta-CD was suggested to penetrate the matrix of the liposomes.

1,2-Dipalmitoylphosphatidylcholine↗
PubMed2002

Thermosetting gels with modulated gelation temperature for ophthalmic use: the rheological and gamma scintigraphic studies.

For ophthalmic drug delivery, Pluronic F127 solutions have a phase transition temperature too low for them to be instilled into the eye at room temperature. Refrigerator storage is usually required to make administration easier, whereas the potential irritation of cold to the sensitive ocular tissues may result in poor topical bioavailability. The purpose of this study is to develop a thermosetting gel with a suitable phase transition temperature by combining Pluronic analogs and to examine the influence of incorporating mucoadhesive polysaccharide, sodium hyaluronate (HA-Na), on the ocular retention of the gel. Dynamic rheological method and single photon emission computing tomography (SPECT) technique were used to ex/in vivo evaluate the thermosetting gels, respectively. An optimized formulation containing 21% F127 and 10% F68 increased the phase transition temperature by 9 degrees C as evaluated by elasticity modulus compared to that of individual 21% F127 solution. Rheological behaviors of the Pluronic solutions showed that the combined Pluronic formulation was free flowing liquid below 25 degrees C and converted to a firm gel under the physiological condition. Furthermore, this formulation possessed the highest viscosity both before and after tear dilution at 35 degrees C. Gamma scintigraphic data demonstrated that the clearance of the thermosetting gel labeled with 99mTc-DTPA was significantly delayed with respect to the phosphate buffered solution, and at least a threefold increase of the corneal residence time was achieved. However, no further improvement in the ocular retention was observed when adding HA-Na into the thermosetting gel due to the substantially decreased gel strength.

Animals↗
PubMed1982

Adamantyl nitroxide: a spin label for probing membrane surfaces.

In an effort to understand more about the perturbing properties of adamantane-like molecules on biological membranes, the spin probe adamantyl nitroxide (2,2'-dimethyl-5-adamantyl oxazolidine-N-oxyl) was synthesized, purified and characterized. Electron paramagnetic resonance (EPR) spectra were then obtained from 1:50 and 1:200 mixtures of adamantyl nitroxide with dipalmitoyl and dipalmityl phosphatidylcholine multibilayers. Above the phase transition temperature of these lipids (41 degrees C for dipalmitoyl phosphatidylcholine and 43 degrees C for dipalmityl phosphatidylcholine) the spectra of adamantyl nitroxide are similar to control spectra obtained in liquid oleic acid. Below the phase transition temperatures, however, spectral differences were observed depending on: (1) the concentration of the spin probe in the lipid; (2) the linkage between the polar head group and the hydrocarbon tails of the phospholipid; (3) the temperature of the sample. Partitioning of adamantyl nitroxide between the aqueous and hydrocarbon phases of the sample is most prominent at probe-to-lipid ratios of 1:200 and at temperatures below the pre-transition temperature of the lipid (around 33 degrees C). Computer simulations of the above results, as well as additional experiments performed at 35 GHz, show that the results arise from true partitioning and not from asymmetric probe motion. Two conclusive results of these experiments are that spectra of adamantyl nitroxide in phospholipid multibilayers are sensitive to probe concentration and to the physical characteristics of the phospholipid which they probe. The spectral differences which arise when adamantyl nitroxide is used with ether- and ester-linked phospholipids indicate that it is a sensitive probe of membrane surfaces. Employment of this molecule in membrane research should prove to be useful in obtaining additional information about membrane surface events.

Adamantane↗
PubMedDate not supplied

Differential scanning calorimetry studies of sebum models.

Human sebum is a mixture of triglycerides, fatty acids, wax esters, squalene, cholesterol, and cholesterol esters. P. acnes, a bacterium that is normally found on the skin, hydrolyzes certain triglycerides to fatty acids, thereby changing the sebum composition. The objective of this study was to examine the physical state of a model sebum and the effect of variations in its composition on its physical properties including (a) the carbon chain length of the components, (b) the ratio of unsaturated to saturated components, and (c) the ratio of triglycerides to fatty acids. A model sebum mixture was prepared based on a composition reported in the literature and evaluated by differential scanning calorimetry (DSC). Since cholesterol and cholesterol esters contribute insignificantly to sebum composition, they were not included. Squalene was kept constant (13%), while the concentration of the rest of the components was varied. Variations of sebum were prepared by dissolving all components in a 3:1 chloroform-methanol mixture for uniformity. Subsequently the solvent was evaporated at room temperature. The samples were then analyzed using DSC. Four distinct endotherms (namely, Mp-1, Mp-2, Mp-3, and Mp-4) were observed between -50 degrees C and 100 degrees C. Mp-1 and Mp-2 occurred below 0 degrees C and were contributed by unsaturated components. Mp-3 and Mp-4, which represent the saturated components, occurred above 30 degrees C. Thus, at normal skin temperature (skin surface temperature is 32 degrees C), sebum contains both a solid and a liquid phase. All the transition temperatures increased with an increase in carbon chain length for the same ratio of unsaturation to saturation. A replacement of unsaturated components with corresponding saturated components led to a decrease in the transition temperatures for the former (Mp-1 and Mp-2) and an increase in the transition temperatures for the latter (Mp-3 and Mp-4). Replacement of triglycerides with corresponding fatty acids (mimicking the action of anaerobic bacteria) caused an increase in Mp-2 and a decrease in Mp-4. In all cases, the final melting temperature (Mp-4) was greater than the temperature of the human skin surface (32 degrees C); thus components contributing to these endotherms are still solids at skin temperature. All variations in the sebum model led to mixtures of solids and liquids at skin temperature. Considering a reduction in Mp-3 and/or Mp-4 to represent sebum "fluidization," it was achieved by a decrease in carbon chain length, an increase in unsaturation, or a substitution of triglycerides by corresponding fatty acids. Preferential enrichment with the saturated species will lead to enrichment of solids versus liquids in the sebum, presumably making it difficult for the liquid phase to dissolve the solids. It seems plausible that perturbation of the balance of solid and liquid components of sebum, such as by P. acnes action, may lead to blockage of the follicle. Future research will investigate strategies to dissolve and/or liquify the solid phase of sebum.

Calorimetry, Differential Scanning↗
PubMed1981

A calorimetric study of the thermotropic behaviour of 1,2-dipentadecylmethylidene phospholipids.

Differential scanning calorimetry was used to study the thermotropic behaviour of 1,2-dipentadecylmethylidene phospholipids with various head groups. The structural variation in the glycerol backbone region leads to a strong restriction of conformational freedom for the first two methylene segments of the chains, so that dipentadecylmethylidene phospholipids show lower transition temperatures, lower enthalpies and lower cooperativity of the transition from the gel to the liquid crystalline phase. The extreme chemical stability of these lipids in the alkaline pH region enables investigations of phosphatidylethanolamine and phosphatidic acid dispersions at high pH values. Both phospholipids show a decrease in the transition temperature and in the transition enthalpy as they become singly and doubly charged, respectively. A complex behaviour of the transition enthalpy of doubly charged 1,2-dipentadecylmethylidene phosphatidic acid was observed when the NaCl concentration of the dispersion was increased.

Calorimetry, Differential Scanning↗
PubMed1991

Enhanced stability of subtilisin by three point mutations.

This study was undertaken to characterize the effect of three point mutations made on aprA-subtilisin on the stability of the protein to both heat- and detergent-induced denaturation. Asparagine residues at positions 109 and 218 were replaced with serine residues to prevent the possible cyclization between these asparagines and the adjacent glycine residues and hence to increase the long-term stability. The effect of these substitutions on conformational stability was examined by thermal denaturation. At high calcium concentrations, the Ser109-substituted analog showed a 3 degrees C higher transition temperature than that of aprA-subtilisin, while the Ser218 substituted analog had a 4 degrees C higher transition temperature. The analog with both changes had a 7 degrees C higher transition temperature than that of the original aprA-subtilisin, indicating that the contributions of the individual mutations were additive. The analog with both mutations also exhibited increased stability in the presence of sodium dodecyl sulfate (SDS) when compared to aprA-subtilisin. In addition to the above two mutations, the asparagine at position 76, located in the high affinity Ca(2+) binding loop of subtilisin, was changed to aspartic acid. The effect of this mutation on the thermal stability of the protein was examined at different calcium concentrations. The analog with all three mutations exhibited little dependence on calcium concentration below 1 mM levels, while the proteins without the mutation at asparagine-76 displayed a strong dependence of melting temperature on Ca(2+) concentration in this range. At much higher calcium concentrations, the analog with three mutations showed an increase in stability similar to that observed with aprA-subtilisin. The analog with three mutations also exhibited greater stability to SDS-induced denaturation than both aprA-subtilisin and the Ser109- and Ser218-substituted analogs. The activation energy barrier for loss of structure in 1% SDS for the analog with all three mutations was increased over that for aprA-subtilisin by 16 kcal/ml. These results suggest that the mutation of asparagine-76 to aspartic acid increases the affinity of the primary Ca(2+) binding site.

Circular Dichroism↗
PubMed2003

Effect of amino acid surfactants on phase transition of poly(N-isopropylacrylamide) gel.

The volume phase transition behavior of a poly(N-isopropylacrylamide) gel (NIPA gel) in solutions of N-acyl amino acid surfactants were studied as a function of surfactant concentration. The addition of a surfactant beyond the critical micelle concentration (cmc) produced elevation in the transition temperature of the NIPA gel and its swelling. The changes in the volume phase transition temperature and in the swelling of the NIPA gel became more significant with the decreasing size of the amino acid side chain. This result could almost be explained only by the binding amount of surfactant onto the NIPA gel regardless of molecular structure of the amino acid. The binding amount increased in the order of sodium N-lauroyl-glycinate>-alaninate>-valinate>-leucinate>or=-phenylalaninate. For an N-acyl amino acid surfactant to bind onto the NIPA gel, to increase the transition temperature, and to facilitate swelling of the gel, the steric hindrance of the amino acid side chain was more effective than its hydrophobicity.

Acrylamides↗
PubMed1980

Thermal dependence of apolipoprotein A-I-phospholipid recombination.

Studies of the recombination of apolipoprotein A-I (apo A-I), the major protein constituent of human high-density lipoprotein, and various synthetic phospholipids, both alone and in mixtures, have been performed. Pure diacyl phospholipids containing homologous fatty acids of the C12, C13, C14, and C15 series, as well as the two positional isomers containing C14 and C16 fatty acids in positions 1 and 2, undergo reaction with the apo A-I protein only near their gel-liquid-crystalline transition temperatures; the degree of reactivity of these phospholipids toward recombination was observed to decrease as the transition temperature increased. The presence of lysolecithin in the incubation mixtures at proportions of 5 mol/mol of protein or lower was not found to have a significant effect on the rate of recombination. Binary mixtures of dimyristoylphosphatidylcholine and dipalmitoylphosphatidylcholine at various proportions react maximally with apo A-I at the onset of the phase transition, as judged by comparison with published phase diagrams; in this case also, the rate of recombination was observed to decline for mixtures with higher phase transition temperatures. These results are interpreted in terms of protein insertion at lattice defects arising from the presence of phospholipid clusters undergoing the phase transition; these clusters are derived from the cooperative and simultaneous melting of a number of molecules, the cooperativity being dependent upon the nature of the phospholipid. It is postulated that phospholipids which melt in a more highly cooperative fashion are more capable of interacting with the apolipoproteins since these phospholipids will possess larger lattice defects during the phase transition.

Apolipoprotein A-I↗
PubMed1994

Temperature change of the ripple structure in fully hydrated dimyristoylphosphatidylcholine/cholesterol multibilayers.

The ripple structure was studied as a function of temperature in fully hydrated dimyristoylphosphatidylcholine (DMPC)/cholesterol multibilayers using synchrotron x-ray small-angle diffraction and freeze-fracture electron microscopy. In the presence of cholesterol, the ripple structure appears below the pretransition temperature of pure DMPC multibilayers. In this temperature range the ripple periodicity is relatively large (25-30 nm) and rapidly decreases with increasing temperature. In this region, defined as region I, we observed coexistence of the P beta' phase and the L beta' phase. The large ripple periodicity is caused by the formation of the P beta' phase region in which cholesterol is concentrated and the L beta' phase region from which cholesterol is excluded. An increase in ripple periodicity also takes place in the narrow temperature range just below the main transition temperature. We define this temperature region as region III, where the ripple periodicity increases dramatically toward the main transition temperature. In region II, between regions I and III, the ripple periodicity decreases gradually with temperature. This behavior is quite similar to that of pure DMPC. Temperature-versus-ripple periodicity curves are parallel among pure DMPC and DMPCs with various cholesterol contents. We explain this behavior in terms of a model proposed by other workers.

Cholesterol↗
PubMed1992

Interaction of membrane phospholipids with some DNA substructures studied by means of differential scanning calorimetry.

The interaction of dipalmitoylphosphatidylcholine, dipalmitoylphosphatidic acid and dipalmitoylphosphatidylethanolamine with some DNA substructures such as cytidine, uridine, adenosine 5'di- and triphosphate, guanosine 5'mono- and diphosphate, cytidine 5'mono- and triphosphate, uridine 5'mono- and triphosphate and inosine 5'monophosphate was studied with differential scanning calorimetry. The dependence of pretransition and main transition temperatures and the enthalpy of main transition on the molecular characteristics of the interacting molecular species was calculated by stepwise regression analysis. Nucleosides and nucleotides increased the main transition temperature and peak half width of phospholipids and they decreased the enthalpy of main transition proving the existence of interaction between phospholipids and DNA substructures. Calculation proved that the interaction is mainly of hydrophilic character but the involvement of hydrophobic forces or steric conditions cannot be ruled out.

Calorimetry, Differential Scanning↗
PubMed1992

Effect of glycolipids on the phase behavior and dynamic properties of phospholipid liposomes.

The glycolipids of Acholeplasma laidlawii AIH089 membranes were identified and purified. The effect of monoglucosyldiacylglycerol (MGDG) and diglucosyldiacylglycerol (DGDG) on the thermotropic behavior of multilamellar vesicles of dipalmitoylphosphatidylcholine (DPPC), dipalmitoylphosphatidylglycerol (DPPG) has been investigated by high sensitivity differential scanning calorimetry. The main transition peaks were broadened, the enthalpies were decreased. DGDG caused the decrease in the transition temperatures of DPPC, DPPG liposomes by 3.08 degrees C, 4.18 degrees C, respectively. MGDG did not cause the alteration of the transition temperature of DPPC liposomes but caused the decrease of the transition temperatures of DPPG liposomes by 2.20 degrees C. ESR experiments indicate that MGDG decreased the rotational correlation time of DPPC and DPPG liposomes.

1,2-Dipalmitoylphosphatidylcholine↗