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. 2021 Aug 2;11:15650. doi: 10.1038/s41598-021-94873-3

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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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Key binding interactions between SARS-CoV-2-RBD (green) and (A) ACE2³⁶, (B) SBP1³⁶, (C) SPB25³⁶, (D) SPB25_K11F, (E) SPB25_Q22R, (F) SPB25_{F8R/K11W//L25R} or (G) SPB25_{F8R/K11F/Q22R/L25R}. The structures of SBP1, SPB25 and designed peptides (pink) were superimposed with ACE2 (grey). Key hydrogen bonds and salt bridges (hydrogen bond occupations > 25%) are shown in blue dashed lines. These structures are the structures closest to the average structures from the 80–100 ns MD trajectories.