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. 2019 Apr 23;9:6440. doi: 10.1038/s41598-019-42867-7

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© The Author(s) 2019

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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Ionic current measurements. (a) The system is constituted by an α- Hemolysin (αHL, blue) nanopore embedded into a lipid membrane (gray). A 35-residues homopeptide (orange chain) is imported into the nanopore with the central residue close to the pore constriction. The simulation box is filled up by 2M KCl electrolyte solution, that, for the sake of clarity, is not shown. A constant and homogeneous external electric field E = (0, 0, E_z) parallel to the pore axis is applied. (b) Average current blockage ΔI/I₀ = (I₀ − I)/I₀, with I the average current measured with the homopeptide inside the pore and I₀ the empty pore value, for four different homopeptides, Ala, Phe, Gln, Trp. The data are obtained averaging the current blockades of five replicas for each homopeptide. Error bars are estimated by considering current blockades from independent replicas as independent measurements. (c) Molecular structure and Van der Waals volume of the four amino acids⁴⁵.