Autocatalytic transport of the peptide antibiotics suzukacillin and alamethicin across lipid membranes

Schindler, Hansgeorg

doi:10.1016/0014-5793(79)81105-9

Cited by 20 publications

(5 citation statements)

References 8 publications

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“…We suggest this occurs because annexin decreases the rate of alamethicin transfer from the trans membrane-aqueous interface to the trans aqueous phase, causing an increase in the surface concentration of alamethicin on the trans side and a consequent increase in the conductance for a given negative voltage. This mechanism is consistent with the known actions of alamethicin (Schindler, 1979;Hall, 1981), the reduction of the nonactin conductance by annexin, and the slowing of the tetraphenylborate translocation rate.…”

Section: Possible Mechanisms Of Annexin Actionsupporting

confidence: 88%

Annexins V and Xii Alter the Properties of Planar Lipid Bilayers Seen by Conductance Probes

Sokolov

Mailliard

Tranngo

et al. 2000

The Journal of General Physiology

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Annexins are proteins that bind lipids in the presence of calcium. Though multiple functions have been proposed for annexins, there is no general agreement on what annexins do or how they do it. We have used the well-studied conductance probes nonactin, alamethicin, and tetraphenylborate to investigate how annexins alter the functional properties of planar lipid bilayers. We found that annexin XII reduces the nonactin-induced conductance to ∼30% of its original value. Both negative lipid and ∼30 μM Ca2+ are required for the conductance reduction. The mutant annexin XIIs, E105K and E105K/K68A, do not reduce the nonactin conductance even though both bind to the membrane just as wild-type does. Thus, subtle changes in the interaction of annexins with the membrane seem to be important. Annexin V also reduces nonactin conductance in nearly the same manner as annexin XII. Pronase in the absence of annexin had no effect on the nonactin conductance. But when added to the side of the bilayer opposite that to which annexin was added, pronase increased the nonactin-induced conductance toward its pre-annexin value. Annexins also dramatically alter the conductance induced by a radically different probe, alamethicin. When added to the same side of the bilayer as alamethicin, annexin has virtually no effect, but when added trans to the alamethicin, annexin dramatically reduces the asymmetry of the I-V curve and greatly slows the kinetics of one branch of the curve without altering those of the other. Annexin also reduces the rate at which the hydrophobic anion, tetraphenylborate, crosses the bilayer. These results suggest that annexin greatly reduces the ability of small molecules to cross the membrane without altering the surface potential and that at least some fraction of the active annexin is accessible to pronase digestion from the opposite side of the membrane.

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Section: Possible Mechanisms Of Annexin Actionsupporting

confidence: 88%

Annexins V and Xii Alter the Properties of Planar Lipid Bilayers Seen by Conductance Probes

Sokolov

Mailliard

Tranngo

et al. 2000

The Journal of General Physiology

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“…In a recent paper, Schindler (1979) has studied the autocatalytic transport of the peptide antibiotics suzukacillin A (an ALA analogue) and ALA RF30 across black lipid membranes. The antibiotic was added to the compartment with the negative pole of the applied electric potential; i.e., the membrane was initially in the nonconductive state.…”

Section: Discussionmentioning

confidence: 99%

Distribution and diffusion of alamethicin in a lecithin/water model membrane system

Fringeli

1980

J. Membrain Biol.

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Attenuated total reflection infrared spectroscopy has been used to determine the equilibrium distribution of the peptide antibiotic alamethicin RF30 between dipalmitoyl phosphatidylcholine bilayers and the aqueous environment. The distribution coefficient K = cWeq/cMeq turned out to be concentration dependent, pointing to alamethicin association in the membrane with increasing concentration in the aqueous phase (cWeq). This concentration was varied within 28 and 310 nM, i.e., in a range typical for black film experiments. Furthermore. diffusion coefficients of alamethicin in the hydrophobic phase of the membrane (DM) and across the membrane/water interface (DI) have been estimated from the time course of the equilibration process. It was found that the diffusion rate of the uncharged analogue RF50 is about 10 times higher than that of the RF30 component, exhibiting one negative charge at the C-terminus. The time constants for transmembrane diffusion of alamethicin RF30 varied between 2.2hr at low concentration and 3.2 hr at higher concentration. The corresponding low concentration value of the RF50 component was found to be 0.25 hr.

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“…At +70 mV, the current becomes regenerative as soon as alamethicin activity begins . equilibration of alamethicin at the inner surface of the membrane (see Schindler, 1979) or perhaps flip-flop of some lipid component induced by alamethicin leading to an increase in the field across the membrane (Hall, 1981) . Regenerative responses are not observed for hyperpolarized voltages from 0 to about -100 mV.…”

Section: Regenerative Current Responsesmentioning

confidence: 99%

Alamethicin channels incorporated into frog node of ranvier: calcium-induced inactivation and membrane surface charges.

Cahalan¹,

Hall²

1982

The Journal of General Physiology

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Alamethicin, a peptide antibiotic, partitions into artificial lipid bilayer membranes and into frog myelinated nerve membranes, inducing a voltage-dependent conductance . Discrete changes in conductance representing single-channel events with multiple open states can be detected in either frog node or lipid bilayer membranes . In 120 mM salt solution, the average conductance of a single channel is approximately 600 pS. The channel lifetimes are roughly two times longer in the node membrane than in a phosphatidylethanolamine bilayer at the same membrane potential . With 2 or 20 mM external Ca and internal CsCl, the alamethicin-induced conductance of frog nodal membrane inactivates . Inactivation is abolished by internal EGTA, suggesting that internal accumulation of calcium ions is responsible for the inactivation, through binding of Ca to negative internal surface charges . As a probe for both external and internal surface charges, alamethicin indicates a surface potential difference of approximately -20 to -30 mV, with the inner surface more negative . This surface charge asymmetry is opposite to the surface potential distribution near sodium channels.

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Autocatalytic transport of the peptide antibiotics suzukacillin and alamethicin across lipid membranes

Cited by 20 publications

References 8 publications

Annexins V and Xii Alter the Properties of Planar Lipid Bilayers Seen by Conductance Probes

Annexins V and Xii Alter the Properties of Planar Lipid Bilayers Seen by Conductance Probes

Distribution and diffusion of alamethicin in a lecithin/water model membrane system

Alamethicin channels incorporated into frog node of ranvier: calcium-induced inactivation and membrane surface charges.

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