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G Cevc

Publications and source records attributed to G Cevc.

44 records · Page 3Linked to original sources
PubMed1984

X-ray diffraction study of the polymorphism of hydrated diacyl- and dialkylphosphatidylethanolamines.

The structure and polymorphism of a homologous series of diacyl- and of dialkylphosphatidylethanolamines have been investigated by X-ray diffraction, calorimetry, and density measurement. The compositional dependence of the repeat spacings of the gel (L beta or L beta'), fluid bilayer (L alpha), and inverted hexagonal (HII) phases has been determined both for the short chain length (di-C12) dialkyl didodecylphosphatidylethanolamine (DDPE) and for the long chain length (di-C20) diacyl diarachinoylphosphatidylethanolamine (DAPE). These data, in conjunction with the measured phase transition temperatures obtained both by X-ray diffraction and by differential scanning calorimetry, have been used to construct phase diagrams for the two lipids. DDPE exhibits metastable behavior in the L beta and L alpha phases below 44 degrees C at all water contents and forms cubic and other nonlamellar phases between the L alpha and HII phases. At low water contents, crystalline and fluid phases coexist at temperatures up to 83 degrees C. For DAPE, the behavior is simpler. In the gel phase, the hydrocarbon chains are tilted at 29 degrees to the bilayer normal, and metastability is only observed at water contents below 3 wt %. The L alpha phase is adopted within a narrow temperature range and then transforms directly to the HII phase. The structural parameters of the L beta (L beta'), L alpha, and HII phases of DDPE and DAPE have been calculated from the X-ray data, in conjunction with the measured values of lipid partial specific volume. In addition, the chain-length dependence of the repeat spacings of the phases has been measured for the homologous series of diacyl and dialkyl lipids. Taken together, the results allow a detailed description of the effects of temperature, hydration, and chain length on the polymorphism of the saturated phosphatidylethanolamines.

Calorimetry↗
PubMed1981

Titration of the phase transition of phosphatidylserine bilayer membranes. Effects of pH, surface electrostatics, ion binding, and head-group hydration.

The dependence of the gel-to-fluid phase transition temperature of dimyristoyl- and dipalmitoylphosphatidylserine bilayers on pH, NaCl concentration, and degree of hydration has been studied with differential scanning calorimetry and with spin-labels. On protonation of the carboxyl group (pK2app = 5.5), the transition temperature increases from 36 to 44 degrees C in the fully hydrated state of dimyristoylphosphatidylserine (from 54 to 62 degrees C for dipalmitoylphosphatidylserine), at ionic strength J = 0.1. In addition, at least two less hydrated states, differing progressively by 1 H2O/PS, are observed at low pH with transition temperatures of 48 and 52 degrees C for dimyristoyl- and 65 and 68.5 degrees C for dipalmitoylphosphatidylserine. On deprotonation of the amino group (pK3app = 11.55) the transition temperature decreases to approximately 15 degrees C for dimyristoyl- and 32 degrees C for dipalmitoylphosphatidylserine, and a pretransition is observed at approximately 6 degrees C (dimyristoylphosphatidylserine) and 21.5 degrees C (dipalmitoylphosphatidylserine), at J = 0.1. No titration of the transition is observed for the fully hydrated phosphate group down to pH less than or equal to 0.5, but it affinity for water binding decreases steeply at pH greater than or equal to 2.6. Increasing the NaCl concentration from 0.1 to 2.0 M increases the transition temperature of dimyristoyphosphatidylserine by approximately 8 degrees C at pH 7, by approximately 5 degrees at pH 13, and by approximately 0 degrees C at pH 1. These increases are attributed to the screening of the electrostatic titration-induced shifts in transition temperature. On a further increase of the NaCl concentration to 5.5 M, the transition temperature increases by an additional 9 degree C at pH 7, 13 degree C at pH 13, approximately 7 degree C in the fully hydrated state at pH 1, and approximately 4 and approximately 0 degree C in the two less hydrated states. These shifts are attributed to displacement of water of hydration by ion binding. From the salt dependence it is deduced that the transition temperature shift at the carboxyl titration can be accounted for completely by the surface charge and change in hydration of approximately 1 H2O/lipid, whereas that of the amino group titration arises mostly from other sources, probably hydrogen bonding. The shifts in pK (delta pK2 = 2.85, delta pK3 = 1.56) are consistent with a reduced polarity in the head-group region, corresponding to an effective dielectric constant epsilon approximately or equal to 30, together with surface potentials of psi congruent to -100 and -150 mV at the carboxyl and amino group pKs, respectively. The transition temperature of dimyristoylphosphatidylserine-water mixtures decreases by approximately 4 degree C each water/lipid molecule added, reaching a limiting value at a water content of approximately 9-10 H2O/lipid molecule.

Calorimetry, Differential Scanning↗
PubMed1980

The caries resistance of human teeth is determined by the spatial arrangement of hydroxyapatite microcrystals in the enamel.

Teeth from different people differ in their susceptibility to caries. The beginning and the development of tooth decay depend on the presence of bacterial plaque and on the structure of the tooth enamel. But it has not been established whether the organic or the inorganic component of the enamel (which is comprised principally of hydroxyapatite microcrystals organized in a firm matrix), is responsible for most of the resistance of teeth to caries. We report here that the electron spin resonance (ESR) lines of the (CO3)3 defect of samples of enamel prepared from caries-resistant teeth differ significantly from the corresponding spectra of the caries-sensitive samples. We have traced these differences to the hydroxyapatite microcrystalline alignment in the tooth enamel, and found that this alignment is specific to individuals and is therefore probably nutritionally or genetically determined.

Crystallography↗
PubMedDate not supplied

Biophysical view of the role of interfaces in biomolecular recognition.

Molecular recognition plays a key role in life. Macromolecular interactions at and with interfaces are of paramount importance in this respect. It is therefore crucial to understand and quantify the forces near the surfaces of biological interest in sufficient detail. Specific binding of large molecules, such as antibodies, is affected by the proximity of polar surfaces, for example. On the one hand, the presence of the net surface charges may raise or lower the local macromolecular concentration depending on the relative sign of the charges involved. On the other hand, the ligands attached to strongly polar surfaces always attract and bind their corresponding antibodies less efficiently than the corresponding dissolved molecules. The reason for this is the non-Coulombic repulsion between the ligand-presenting polar surface and the approaching macromolecule. This force is promoted by the surface hydrophilicity and the width of the interfacial region. A simple, direct hydration force is seldom, if ever, seen in such systems. (This is owing to the very short range (Lambda (h ) reverse similar 0.1 nm ) of pure hydration force.) The non-specific adsorption of proteins to the lipid bilayer is also little affected by the overall repulsion between the macromolecule and the bilayer surface; such an adsorption is governed more by the number of defects and/or by the availability of the hydrophobic binding sites in the interfacial region. Artificial lipid membranes typically offer numerous such binding sites to the surrounding macromolecules. Multiple non-specific protein adsorption, which results in partial macromolecular denaturation or complement activation, is therefore one of the main reasons for the rapid elimination of lipid vesicles from the blood stream in vivo. To promote the circulation time of an intravenously injected lipid suspension it is therefore necessary to modify the surfaces of their constituent lipid bilayers. Increasing the surface net charge density and/or increasing the bilayer surface hydrophilicity is of little use in this respect. In order to affect the non-specific bilayer-protein interactions significantly, an optimal number of water-soluble, short and sufficiently mobile polymers must be attached to the lipid head-groups. These polymers then increase the repulsive barrier of the membrane surface dramatically, due to the generation of a thick and mobile as well as strongly hydrated interface. Owing to this, the affinity for proteins of the resulting surface is lowered and the surface-induced protein denaturation or complement insertion is hampered. Polymer-coated liposomes, consequently, are not attractive for the phagocytic cells. Such liposomes, consequently, remain in the blood circulation much longer than simple lipid vesicles; the former, consequently, may spontaneously accumulate in tumors.

Journal Article↗
PubMedDate not supplied

Transdermal immunisation with an integral membrane component, gap junction protein, by means of ultradeformable drug carriers, transfersomes.

Molecules greater than 500 Da normally do not cross the skin. This prevents epicutaneous delivery of the high molecular weight therapeutics as well as non-invasive transcutaneous immunisation. Extremely deformable vesicles prepared by the judicious combination of several materials provide a solution to this problem: the resulting agent carriers, transfersomes, are the only tested colloidal system that can transport even large macromolecules spontaneously through the skin in immunologically active form. Gap junction proteins (GJP) incorporated into transfersomes and applied to the intact skin surface thus give rise to specific antibody titres marginally higher than those elicited by subcutaneous injections of GJP in transfersomes, mixed lipid micelles or liposomes. The latter two carrier systems give no significant biological response after epicutaneous administration. Transcutaneous protein delivery by means of transfersomes also appears to increase the relative concentration of anti-GJP IgA in the serum.

Administration, Topical↗