Cationic Polymers Inhibit the Conductance of Lysenin Channels

The pore-forming toxin lysenin self-assembles large and stable conductance channels in natural and artificial lipid membranes. The lysenin channels exhibit unique regulation capabilities, which open unexplored possibilities to control the transport of ions and molecules through artificial and natura...

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Main Authors: Daniel Fologea, Eric Krueger, Steve Rossland, Sheenah Bryant, Wylie Foss, Tyler Clark
Format: Article
Language:English
Published: Hindawi Limited 2013-01-01
Series:The Scientific World Journal
Online Access:http://dx.doi.org/10.1155/2013/316758
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spelling doaj-ea200d1862a7406a957ed11af7f3497d2020-11-25T00:50:37ZengHindawi LimitedThe Scientific World Journal1537-744X2013-01-01201310.1155/2013/316758316758Cationic Polymers Inhibit the Conductance of Lysenin ChannelsDaniel Fologea0Eric Krueger1Steve Rossland2Sheenah Bryant3Wylie Foss4Tyler Clark5Boise State University, Department of Physics, 1910 University Drive, Boise, ID 83725-1570, USABoise State University, Department of Physics, 1910 University Drive, Boise, ID 83725-1570, USABoise State University, Department of Physics, 1910 University Drive, Boise, ID 83725-1570, USABoise State University, Department of Physics, 1910 University Drive, Boise, ID 83725-1570, USABoise State University, Department of Physics, 1910 University Drive, Boise, ID 83725-1570, USABoise State University, Department of Physics, 1910 University Drive, Boise, ID 83725-1570, USAThe pore-forming toxin lysenin self-assembles large and stable conductance channels in natural and artificial lipid membranes. The lysenin channels exhibit unique regulation capabilities, which open unexplored possibilities to control the transport of ions and molecules through artificial and natural lipid membranes. Our investigations demonstrate that the positively charged polymers polyethyleneimine and chitosan inhibit the conducting properties of lysenin channels inserted into planar lipid membranes. The preservation of the inhibitory effect following addition of charged polymers on either side of the supporting membrane suggests the presence of multiple binding sites within the channel's structure and a multistep inhibition mechanism that involves binding and trapping. Complete blockage of the binding sites with divalent cations prevents further inhibition in conductance induced by the addition of cationic polymers and supports the hypothesis that the binding sites are identical for both multivalent metal cations and charged polymers. The investigation at the single-channel level has shown distinct complete blockages of each of the inserted channels. These findings reveal key structural characteristics which may provide insight into lysenin’s functionality while opening innovative approaches for the development of applications such as transient cell permeabilization and advanced drug delivery systems.http://dx.doi.org/10.1155/2013/316758
collection DOAJ
language English
format Article
sources DOAJ
author Daniel Fologea
Eric Krueger
Steve Rossland
Sheenah Bryant
Wylie Foss
Tyler Clark
spellingShingle Daniel Fologea
Eric Krueger
Steve Rossland
Sheenah Bryant
Wylie Foss
Tyler Clark
Cationic Polymers Inhibit the Conductance of Lysenin Channels
The Scientific World Journal
author_facet Daniel Fologea
Eric Krueger
Steve Rossland
Sheenah Bryant
Wylie Foss
Tyler Clark
author_sort Daniel Fologea
title Cationic Polymers Inhibit the Conductance of Lysenin Channels
title_short Cationic Polymers Inhibit the Conductance of Lysenin Channels
title_full Cationic Polymers Inhibit the Conductance of Lysenin Channels
title_fullStr Cationic Polymers Inhibit the Conductance of Lysenin Channels
title_full_unstemmed Cationic Polymers Inhibit the Conductance of Lysenin Channels
title_sort cationic polymers inhibit the conductance of lysenin channels
publisher Hindawi Limited
series The Scientific World Journal
issn 1537-744X
publishDate 2013-01-01
description The pore-forming toxin lysenin self-assembles large and stable conductance channels in natural and artificial lipid membranes. The lysenin channels exhibit unique regulation capabilities, which open unexplored possibilities to control the transport of ions and molecules through artificial and natural lipid membranes. Our investigations demonstrate that the positively charged polymers polyethyleneimine and chitosan inhibit the conducting properties of lysenin channels inserted into planar lipid membranes. The preservation of the inhibitory effect following addition of charged polymers on either side of the supporting membrane suggests the presence of multiple binding sites within the channel's structure and a multistep inhibition mechanism that involves binding and trapping. Complete blockage of the binding sites with divalent cations prevents further inhibition in conductance induced by the addition of cationic polymers and supports the hypothesis that the binding sites are identical for both multivalent metal cations and charged polymers. The investigation at the single-channel level has shown distinct complete blockages of each of the inserted channels. These findings reveal key structural characteristics which may provide insight into lysenin’s functionality while opening innovative approaches for the development of applications such as transient cell permeabilization and advanced drug delivery systems.
url http://dx.doi.org/10.1155/2013/316758
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AT sheenahbryant cationicpolymersinhibittheconductanceoflyseninchannels
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