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. 2021 Jun 18;12:3741. doi: 10.1038/s41467-021-24122-8

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© The Author(s) 2021

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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Fig. 4 — a Electron density profiles before and after biotin–avidin bindings. b Electron density difference (Δρ = ρ_{SLB + avidin} − ρ_SLB). c Electric field change. d Chemical potential difference upon biotin–avidin binding. e MD simulation of the SLB under avidin binding. The DOPC lipids, B-PE lipids, avidin, and water molecules are colored in green, red, purple, and cyan, respectively. f Induced potential difference upon biotin–avidin binding obtained from MD simulation (see Supplementary Note 11 for details). g Sensor responses to different analytes at identical concentrations. (Av. avidin, S.Av. streptavidin, and N.Av. neutrAvidin). The measurement values represent the mean ± SD for n = 3 independent experiments. Source data are provided as a Source Data file.