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PubMedDate not supplied

[Effect of valinomycin on the phase state and passive permeability for calcium ions of membranes from artificial phospholipids].

Effect of valinomycin on passive permeability for calcium ions of liposomes from artificial phospholipids of dimiristoillecithin and dipalmitoillecithin under the conditions of thermotropic structural transitions which were controlled by means of fluorescent probe of 3-metoxibenzantron. It was found that the incorporating of valinomycin into the membrane depends on the density of phospholipid packing. The change of the physical state of phospholipids under the effect of antibiotic was correlated with the change of passive permeability of liposomes for calcium ions.

Calcium↗
PubMed1980

[Change in the state of a lecithin molecular layer at the heptane-aqueous KCl solutions interface on the introduction of the ionophore, valinomycin].

The influence of ionophore--valinomycin on the organization of the lipid layer located between a heptane solution of lecithin and KCl water solutions of different concentrations has been shown by measurements of the interfacial tension. Specific changes in the interfacial tension found at high KCl concentrations are related to the transition of valinomycin into a form of its complex with K+-ion. A conclusion on the difference in the lipid layer organisation in the presence of the neutral ionophore and its charged complex has been made.

Cations, Monovalent↗
PubMed1995

[Crystalline and molecular structure of the K+-complex of meso-valinomycin, cyclo(-(D-Val-L-Hyi-L-Val-D-Hyi)3-).KAuCl4].

Crystal structure of the complex of meso-valinomycin with KAuCl4 (C60H102N6O18KAuCl4) was determined using direct X-ray diffraction analysis. The conformational state of the complex is similar to that determined earlier for free meso-valinomycin. Characteristic of it is the centrosymmetric bracelet shape stabilized by six intramolecular NH...OC hydrogen bonds of 4 --> 1 type. The K+ ion is located in an inner negatively charged octahedral cavity formed by six carbonyl oxygen atoms of ester groups. The observed differences in conformational angles of the complex and free are caused by readjustment of the geometry of the ion-binding cavity to the size of the ion bound during complexation.

Amino Acid Sequence↗
PubMed1970

Solution conformation of valinomycin-potassium ion complex.

The complete conformation of the valinomycin-potassium ion complex in methanol is presented. Extension from the reported secondary structure requires arguments and data relating to ester orientation, direction of coiling, side-chain orientation, and conformational stability. Conformation of the valinomycin-potassium ion complex provides a clear-cut example in which elucidation of conformation is sufficient to gain an understanding of molecular function which, in this case, is selective ion transport by a carrier mechanism.

Anti-Bacterial Agents↗
PubMed1997

The X-ray structure of the monoclinic crystal form of [D-Hyi2, L-Hyi4] meso-valinomycin.

The conformation and intermolecular association of [D-Hyi2, L-Hyi4] meso-valinomycin [cyclo[-D-Val-D-Hyi-L-Val-L-Hyi-(D-Val-L-Hyi-L-Val-D-+ ++Hyi)2-], C60H102N6O18] in a crystal form obtained from ethanol solution has been determined by x-ray crystallography. Two depsipeptides and one ethanol molecule per asymmetric unit crystallize in space group P2(1) (Z = 4); a = 14.579, b = 39.795, c = 13.928 A, beta = 116.90, Rl = 0.0757. The molecular conformation is very similar to that observed in the trigonal P3(2) crystal form obtained from acetone solution [V. Z. Pletnev et al. (1991) Biopolymers, Vol. 31, pp. 409-415]. Both independent molecules in the crystal adopt a similar distorted bracelet structure with a sterically inaccessible, partially formed, ion-binding center that is stabilized by six 4-->1 type H bonds. The observed conformation accounts for the inability of the molecule to complex ions. Close examination of the three crystallographically independent molecules reveals that differences in the backbone conformation associated with solvent interaction are significantly larger than those associated with hydrophobic van der Waals interactions of crystal packing.

Crystallization↗
PubMed1995

Crystal and molecular structure of the centrosymmetric meso-valinomycin analogue--cyclo (D-Val-D-Hyi-D-Val-L-Hyi-L-Val-D-Hyi-L-Val-L-Hyi-L-Val-D-Hyi-D-Val-L-Hy i) (C60H102N6O18).

The crystal structure of cyclo (D-Val-D-Hyi-D-Val-L-Hyi-L-Val-D-Hyi-L-Val-L-Hyi -L-Val-D-Hyi-D-Val-L-Hyi).2H2O has been solved by x-ray direct methods. The crystals (grown from a mixture of octane/CH2Cl2) are an orthorhombic, centrosymmetric space group Pbca, cell parameters a = 11.458 (2), b = 25.613 (3), c = 23.691 (3) A, Z = 4; therefore the molecule lies on a center of inversion in the cell. The atomic coordinates for the C, N, and O atoms were refined in the anisotropic thermal motion approximation (allowing for H-atom contribution to Fcal) to a standard R-factor value of 0.081. In contrast to meso-valinomycin, the analogue under study does not adopt an octahedral cage bracelet conformation. It has an unusual centrosymmetric elongated form with two type II terminal beta-bends formed by N-H ... C=O 4-->1 type intramolecular H bonds. Two symmetry-related water molecules reside in the elongated molecular cavity of the centrosymmetric depsipeptide ring.

Crystallization↗
PubMed1991

Synergistic cytotoxic actions of cisplatin and liposomal valinomycin on human ovarian carcinoma cells.

We have previously shown that the toxicity of valinomycin (VM), a membrane-active agent with antineoplastic activity, can be dramatically reduced with no loss of the antitumor efficacy of the drug by incorporating it into liposomes. In the present study, we investigated the interaction between cis-diamminedichloroplatinum(II) (CDDP) and VM in terms of in vitro cytotoxicity to human ovarian tumor cells. Using the MTT assay and analyzing the data using the median-effect principle, we showed that synergistic cytotoxic interactions exist between CDDP and VM in their liposomal form. The degree of cytotoxic synergism was influenced by the duration of drug exposure and the dose ratio. The cellular accumulation of platinum by ovarian cells at 37 degrees C was slightly higher after exposure to VM as compared with controls; however, it is not clear that this accounts for the cytotoxic synergism. These results suggest that the combination of liposomal VM and CDDP may have merit as a form of localized drug delivery for the treatment of ovarian cancer disseminated within the peritoneal space.

Antineoplastic Combined Chemotherapy Protocols↗
PubMedDate not supplied

An extended kinetic analysis of valinomycin-induced Rb-transport through monoglyceride membranes.

The time course of the current following a voltage jump, which is applied to monoglyceride bilayers in the presence of valinomycin, shows two relaxation times. This is basically in agreement with a simple carrier model which has been described in full detail formerly. Relaxation times and amplitudes allow a calculation of the rate constants of the transport model. The presented data supplement an analysis which was hitherto based only on the slower relaxation process and on information derived from the nonlinearity of current-voltage characteristics. The additional resolution of the faster relaxation time allowed an approximate determination of the voltage dependence of the translocation rate constant for carrier-ion-complex and provided evidence for a small voltage dependence of the interfacial reaction. The dependence of the relaxation parameters on the ion concentration in the aqueous phase was interpreted assuming a saturation of the ion concentration at the reaction plane at high bulk concentrations.

Biological Transport↗
PubMed1977

Charge ulse studies of transport phenomena in bilayer membranes. II. Detailed theory of steady-state behavior and application to valinomycin-mediated potassium transport.

The charge-pulse technique is applied to a study of valinomycin-mediated potassium transport across glycerol monooleate (GMO) bilayers. The theory, based on the Läuger-Stark model, is developed for the steady-state domain. The voltage dependences of the surface complexation reactions are also considered. The analysis of the data yields the folowing values for the rate constants: (see article). With the exception of this last ratio, all the values agree well with previously published data. The implication of the exponential term, 0.045, is that the plane of reaction for the surface complexation actually occurs a small distance within the membrane dielectric. If one presumes that the reaction plane is about half way between the plane of adsorbed complex and the membrane-water interface, one deduces that the complex "feels" only about 80% of the applied voltage across the membrane.

Biological Transport↗
PubMed1975

Charge pulse studies of transport phenomena in bilayer membranes. I. Steady-state measurements of actin- and valinomycin-mediated transport in glycerol monooleate bilayers.

A charge pulse technique has been applied to studies of transport phenomena in bilayer membranes. The membrane capacitance can be rapidly charged (in less than a microsecond). The charge then decays through the membrane's conductive mechanism-no current flows through the solution or external circuitry. The resulting voltage decay is thus a manifestation of membrane and boundary layer phenomena only. There are a number of advantages to this approach over conventional voltage or current-clamp techniques: the rise-time of the voltage perturbation is not limited by the time constant deriving from the membrane capacitance and solution resistance, thus permitting study of extremely rapid rate processes; the membrane is exposed to high voltage for relatively short times and thus can be subjected to higher voltages without breakdown; the steady-state current-voltage behavior of the membrane can be deduced from a single charge pulse experiment; the charge (and therefore the integral of the ion flux through the membrane) is monitored allowing detection of rate processes too rapid to follow directly. In this paper we present what is primarily a steady-state analysis of actin (non-, mon-, din-, trin-)-mediated transport of ammonium ion and valinomycin-mediated transport of cesium and potassium ions through glycerol monooleate bilayers. We introduce the concept of the "intercept discrepancy", a method for measuring charge lost through extremely rapid rate processes. Directly observable pre-steady-state phenomena are also discussed but will be the main subject of part II.

Actins↗
PubMed1977

Temperature-jump experiments on thin lipid membranes in the presence of valinomycin.

Temperature jump relaxation experiments on planar lipid membranes in the presence of valinomycin were performed using the absorption of a strong light flash as an energy source for the generation of the T-jump. The relaxation of the current carried by valinomycin/Rb+ complexes was measured. The results were interpreted on the basis of a transport model which was also analyzed by voltage jump relaxation experiments. The study shows that the application of the T-jump technique provides valuable information about transport kinetics as well as the dynamics of the membrane structure. At the given experimental conditions the relaxation of the current is believed to reflect a temperature-dependent transition of the membrane to a new conformational state of low order. The relaxation could be resolved with the present technique only at low temperatures and for membranes of high microviscosity.

Biological Transport↗
PubMed1985

Failure of an alkalophilic bacterium to synthesize ATP in response to a valinomycin-induced potassium diffusion potential at high pH.

Starved whole cells of the obligately alkalophilic Bacillus firmus RAB synthesize ATP upon addition of L-malate at pH 9.0 as expected of an aerobic organism that grows oxidatively on nonfermentable carbon sources at pH values as high as 11.0. The current study was a detailed examination of the perplexing inability of such cells to exhibit ATP synthesis in response to a valinomycin-mediated potassium diffusion potential at pH 9.0. While there were minor differences in the patterns of generation of the potential and the proton influx that accompanies its generation in the three different buffering systems employed, the magnitude of the transmembrane electro-chemical potential of protons was at least as high as pH 9.0 as at pH 7.0. Nevertheless, a diffusion potential consistently energized ATP synthesis at pH 7.0 but not at 9.0; these findings were independent of the presence or absence of Tris or of Na+. By contrast, the artificial electron donor ascorbate, in the presence of phenazine methosulfate, energized ATP synthesis by the starved whole cells at both pH values. The same phenomenon, i.e., efficacy of a respiration-derived potential but not of a diffusion potential at pH 9.0, was demonstrated in ADP + Pi-loaded membrane vesicles. On the other hand, electrogenic Na+-coupled solute transport could be energized by both ascorbate/phenazine and methosulfate and a diffusion potential in the vesicles at pH 9.0. The results are discussed in connection with models of a localized path of proton flow between proton pumps and the ATP synthase.

Adenosine Diphosphate↗
PubMed1982

Membrane potential in a potassium transport-negative mutant of Escherichia coli K-12. The distribution of rubidium in the presence of valinomycin indicates a higher potential than that of the tetraphenylphosphonium cation.

The membrane potential across the cytoplasmic membrane of EDTA-treated cells of a K+ transport-negative mutant of Escherichia coli K-12 was estimated from the equilibrium distribution of different lipid-soluble cations. With glucose as a substrate and at low K+ out, the membrane potential calculated from the distribution ratio of 86Rb+ in the presence of valinomycin (delta psi rb+) was considerably higher than that indicated by the [3H]tetraphenylphosphonium cation (delta psi TPP+). The lipid-soluble anion phenyldicarbaundecaborane (PCB-) increased delta psi TPP+ close to delta psi Rb+. To investigate whether these results were due to different binding of the cations to cellular components, residual Rb+ and TPP+ uptake was measured in cells permeabilized with 5% n-butanol (by volume). In those cells the distribution ratios or Rb+, K+ and Na+ approached a value of 4, indicating that the uptake of all three ions was driven by a residual negative surface potential or transmembrane Donnan potential (internally negative). The distribution ratio of TPP+ was 3--4-times higher than that of other cations and up to 10 mM TPP+ out was almost independent of the added TPP+ concentration. This extra uptake presumably represents binding of TPP+ to the cellular membranes. Thus, at pH 7.5, delta psi Rb+ was about 180--200 mV, whereas after correction for binding delta psi TPP+ was 110--150 and 150--170 mV in the absence and presence of PCB-, respectively. It is proposed that TPP+ indicates too low a potential, because by its strong binding it decreases the negative surface potential of the cytoplasmic membrane, and thereby inhibits its own further uptake. This is taken to mean that TPP+ distribution can be used as a qualitative probe only for the bacterial membrane potential.

Cell Membrane↗
PubMed1976

Stacking of safranine in liposomes during valinomycin-induced efflux of potassium ions.

Liposomes were prepared from phosphatidylcholine and cardiolipin in a KCl medium and suspended in a choline chloride medium with safranine. When efflux of K+ was induced by valinomycin, spectral shifts characteristic of stacking were observed. Ca2+ inhibited the rate of stacking in a competitive manner with a Ki of about 200 muM, while La3+ was about 10 times more potent. When liposomes were prepared from phospholipids with a higher ratio of cardiolipin to phosphatidylcholine the inhibition was more potent. No effect on the stacking phenomena was seen when CA2+ was added after the stacking was completed. When CA2+ or an organic cation with four charges, spermine was trapped in the intraliposomal compartment, no significant change in the rate of stacking was seen. However, the extent of stacking was decreased. It is suggested that safranine is driven by a diffusion potential to a site that is inaccessible to CA2+ in the medium, presumably to the inner boundaries of the liposomal membranes.

Binding Sites↗
PubMed1983

Somatostatin and insulin secretion from pancreatic islets: studies on the effect of high K+, 9-aminoacridine and valinomycin.

We attempted to determine whether a decrease in the potassium permeability of the D cell membrane plays a role in the stimulus-secretion coupling, as it does in the pancreatic B cell. Elevation in the extracellular potassium concentration from 5.5 to 16.5 mM, or 0.2 mM 9-aminoacridine, which decreases potassium permeability in plasma membrane, stimulated the release of somatostatin as well as insulin from the isolated rat pancreatic islets. Valinomycin (1 microM), a potassium ionophore inhibited the secretion in response to high glucose, high extracellular potassium or 9-aminoacridine. These findings indicate that a reduction in potassium permeability in the D cell membrane, as induced by glucose or other stimulants, may be a major step in secretion of somatostatin.

Aminacrine↗
PubMed1995

Sensitivity of valinomycin-based K(+)-selective micro-electrodes to inhibitors of K+ transport.

The sensitivies of double-barrelled K(+)-selective micro-electrodes (KSMs) employing the low-impedance membrane cocktail based on the neutral K(+)-selective ion carrier valinomycin (Fluka, Cocktail B 60398) to the following 3 different classes of inhibitors of K+ transport were measured: (1) general metabolic inhibitors (dinitrophenol, potassium cyanide, sodium azide, rotenone, dicyclohexylcarbodiimide, salicylhydroxamic acid); (2) P-type ATPase inhibitors (vanadate, ouabain, amiloride, SCH 28080); and (3) anion-dependent K+ transport inhibitors (bumetanide, 4-acetamide-4-isothiocyanostilbene-2,2-disulphonic acid). Of the 12 inhibitors tested, only dinitrophenol had any significant effect on the response of KSMs to K+ activity. Comparison of the calibrations in solutions with and without 0.1 mM dinitrophenol showed that this inhibitor behaved as a 'classical' interferent whereby its contribution to the K+ activity signal was statistically significant at K+ activities of 36.0 mM and less. However, at higher K+ activities (97.0 mM), dinitrophenol interference was not significant. It was possible to correct for the DNP interference and to obtain measurements of intracellular K+ activity in insect muscles.

Adenosine Triphosphatases↗
PubMed1995

Application of a fast charge-pulse technique to study the effect of the dipolar substance 2,4-dichlorophenoxyacetic acid on the kinetics of valinomycin mediated K(+)-transport across monoolein membranes.

We report on a modified charge-pulse relaxation technique applied at planar lipid membranes. The method has an improved time resolution of 20-30 ns. It is based on the capacitive coupling of a voltage-jump to the membrane. The method was used to study the fast relaxation processes induced by valinomycin/K+ in the presence of 2,4-dichlorophenoxyacetic acid (2,4-D). The change of the rate constants of the ion carrier valinomycin was analysed as a consequence of the adsorption of the dipolar substance 2,4-D to the membrane/water interface of monoolein membranes. The effect of 2,4-D can be explained solely via the influence of the introduced dipole potential, VD. The latter was found to act (primarily) on the inner membrane barrier experienced by the positively charged carrier-ion complex and on the interfacial barriers responsible for complex formation and dissociation. No evidence for a change of the microviscosity of the membrane interior was obtained.

2,4-Dichlorophenoxyacetic Acid↗