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. 2017 May 26;7:2448. doi: 10.1038/s41598-017-02438-0

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Interaction of Ang II with single lysenin channels inserted into lipid membranes bathed by 1 M KCl solutions buffered with 10 mM Tris and 1 mM EDTA at pH 6.9. (a) Insertion of a single channel in the bilayer membrane was observed as a step change in the ionic current at −60 mV transmembrane potential (sampling time 1 s, 1 kHz low pass hardware filter, and 10 Hz low pass software filter). No transient changes in the ionic current established through two open lysenin channels were observed at −80 mV when: (b) no Ang II was added to the solutions, and (c) Ang II was added to the trans reservoir. (d) Addition of Ang II to the cis reservoir yielded multiple transient changes in the ionic current, indicative of interactions between the channel and peptides. The traces shown in panels (b–d) have been recorded with a sampling time of 4 μs and a 10 kHz low pass hardware filter.