Action on ileal smooth muscle of synthetic detergents and pardaxin

Primor, Naftali

doi:10.1016/0306-3623(86)90183-7

Cited by 5 publications

(2 citation statements)

References 25 publications

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“…Similarly, addition of up to lo-' M pardaxin (PX, arrows) did not alter NBD fluorescence. The slight increase in NBD fluorescence at 1Om6 M pardaxin is probably related to its surfactant properties [20]. However, this surfactant property did not cause sizable disruption of the membrane as seen from the steep increase in NBD fluorescence upon addition of 0.1% Triton X-100.…”

Section: Evaluation Of Pardaxin-mediated Leakage Ofmentioning

confidence: 89%

“…Control liposomes were shown to undergo fusion upon addition of 5 mM calcium ( fig.4B, inset). Previous studies have indicated that at these high concentrations pardaxin might act as a surfactant [20]; however, its mechanism of action seems to differ from that of other detergents, such as Triton, which completely disrupt the vesicles, resulting in an abrupt increase in the NBD fluorescence [21].…”

Section: Evaluation Of Pardaxin-mediated Leakage Ofmentioning

confidence: 99%

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Pardaxin induces aggregation but not fusion of phosphatidylserine vesicles

Lelkes

Lazarovici

1988

FEBS Letters

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The effects on membranes of pardaxin, an amphipathic polypeptide, purified from the gland secretion of the Red Sea Moses sole flatfish Purdachirus marmoratus are dosedependent and range from formation of voltage-gated, cation-selective pores to lysis. We have now investigated the interactions of pardaxin with small unilamellar liposomes. Light scattering showed that pardaxin (10-7-10-9 M) mediated the aggregation of liposomes composed of phosphatidylserine but not of phosphatidylcholine. Aggregation of phosphatidylserine vesicles was impaired by vesicle depolarization. Furthermore, pardaxin-mediated aggregation between fluorescent-labeled PS vesicles was accompanied by leakage of the vesicle contents, and not by fusogenic process within the aggregates. We suggest that pardaxin is a unique polypeptide, that induces vesicle aggregation and membrane destabilization, but not membrane fusion; the mechanism of the aggregation activity of pardaxin is related to its amphipathic properties.

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Section: Evaluation Of Pardaxin-mediated Leakage Ofmentioning

confidence: 89%

Section: Evaluation Of Pardaxin-mediated Leakage Ofmentioning

confidence: 99%