Kalata B1 and Kalata B2 Have a Surfactant-Like Activity in Phosphatidylethanolomine-Containing Lipid Membranes

Cyclotides are cyclic disulfide-rich peptides that are chemically and thermally stable and possess pharmaceutical and insecticidal properties. The activities reported for cyclotides correlate with their ability to target phosphatidylethanolamine (PE)-phospholipids and disrupt cell membranes. However...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1985. - 33(2017), 26 vom: 05. Juli, Seite 6630-6637
1. Verfasser: Cranfield, Charles G (VerfasserIn)
Weitere Verfasser: Henriques, Sónia Troeira, Martinac, Boris, Duckworth, Paul, Craik, David J, Cornell, Bruce
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2017
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Cyclotides Lipid Bilayers Surface-Active Agents kalata B1 kalata B2
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520 |a Cyclotides are cyclic disulfide-rich peptides that are chemically and thermally stable and possess pharmaceutical and insecticidal properties. The activities reported for cyclotides correlate with their ability to target phosphatidylethanolamine (PE)-phospholipids and disrupt cell membranes. However, the mechanism by which this disruption occurs remains unclear. In the current study we examine the effect of the prototypic cyclotides, kalata B1 (kB1) and kalata B2 (kB2), on tethered lipid bilayer membranes (tBLMs) using swept frequency electrical impedance spectroscopy. We confirmed that kB1 and kB2 bind to bilayers only if they contain PE-phospholipids. We hypothesize that the increase in membrane conduction and capacitance observed upon addition of kB1 or kB2 is unlikely to result from ion channel like pores but is consistent with the formation of lipidic toroidal pores. This hypothesis is supported by the concentration dependence of effects of kB1 and kB2 being suggestive of a critical micelle concentration event rather than a progressive increase in conduction arising from increased channel insertion. Additionally, conduction behavior is readily reversible when the peptide is rinsed from the bilayer. Our results support a mechanism by which kB1 and kB2 bind to and disrupt PE-containing membranes by decreasing the overall membrane critical packing parameter, as would a surfactant, which then opens or increases the size of existing membrane defects. The cyclotides need not participate directly in the conductive pore but might exert their effect indirectly through altering membrane packing constraints and inducing purely lipidic conductive pores 
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650 4 |a Research Support, Non-U.S. Gov't 
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650 7 |a Lipid Bilayers  |2 NLM 
650 7 |a Surface-Active Agents  |2 NLM 
650 7 |a kalata B1  |2 NLM 
650 7 |a kalata B2  |2 NLM 
700 1 |a Henriques, Sónia Troeira  |e verfasserin  |4 aut 
700 1 |a Martinac, Boris  |e verfasserin  |4 aut 
700 1 |a Duckworth, Paul  |e verfasserin  |4 aut 
700 1 |a Craik, David J  |e verfasserin  |4 aut 
700 1 |a Cornell, Bruce  |e verfasserin  |4 aut 
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